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- EMDB-10751: AP2 in clathrin coats assembled on a membrane containing dileucin... -

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Basic information

Entry
Database: EMDB / ID: EMD-10751
TitleAP2 in clathrin coats assembled on a membrane containing dileucine- and tyrosine-based cargo peptides
Map dataSharpened map of AP2 in clathrin coat formed on membranes containing dileucine- and tyrosine-based cargo peptides
Sample
  • Complex: Clathrin/AP2 coat assembled on AP2 membrane.
    • Complex: AP-2 complex in clathrin coat, subunits alpha-2 and mu
      • Protein or peptide: AP-2 complex subunit alpha-2
      • Protein or peptide: AP-2 complex subunit mu
    • Complex: AP-2 complex in clathrin coat, subunit beta
      • Protein or peptide: AP-2 complex subunit beta
    • Complex: AP-2 complex in clathrin coat, subunit sigma
      • Protein or peptide: AP-2 complex subunit sigma
Keywordsclathrin / clathrin adaptor / ap2 / clathrin assembly / ENDOCYTOSIS
Function / homology
Function and homology information


Gap junction degradation / Formation of annular gap junctions / LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / Retrograde neurotrophin signalling / Nef Mediated CD8 Down-regulation / Trafficking of GluR2-containing AMPA receptors ...Gap junction degradation / Formation of annular gap junctions / LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / Retrograde neurotrophin signalling / Nef Mediated CD8 Down-regulation / Trafficking of GluR2-containing AMPA receptors / VLDLR internalisation and degradation / Retrograde neurotrophin signalling / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / Trafficking of GluR2-containing AMPA receptors / WNT5A-dependent internalization of FZD4 / VLDLR internalisation and degradation / extrinsic component of presynaptic endocytic zone membrane / clathrin adaptor complex / WNT5A-dependent internalization of FZD4 / Recycling pathway of L1 / MHC class II antigen presentation / AP-2 adaptor complex / regulation of vesicle size / postsynaptic neurotransmitter receptor internalization / Cargo recognition for clathrin-mediated endocytosis / Recycling pathway of L1 / Retrograde neurotrophin signalling / clathrin-coated endocytic vesicle / Clathrin-mediated endocytosis / positive regulation of synaptic vesicle endocytosis / Cargo recognition for clathrin-mediated endocytosis / clathrin adaptor activity / Clathrin-mediated endocytosis / LDL clearance / membrane coat / vesicle budding from membrane / clathrin-dependent endocytosis / MHC class II antigen presentation / signal sequence binding / coronary vasculature development / Nef Mediated CD4 Down-regulation / endolysosome membrane / aorta development / ventricular septum development / Neutrophil degranulation / clathrin binding / low-density lipoprotein particle receptor binding / Trafficking of GluR2-containing AMPA receptors / Recycling pathway of L1 / positive regulation of receptor internalization / synaptic vesicle endocytosis / EPH-ephrin mediated repulsion of cells / negative regulation of protein localization to plasma membrane / vesicle-mediated transport / clathrin-coated pit / protein serine/threonine kinase binding / phosphatidylinositol binding / MHC class II antigen presentation / VLDLR internalisation and degradation / kidney development / intracellular protein transport / clathrin-coated endocytic vesicle membrane / terminal bouton / receptor internalization / cytoplasmic side of plasma membrane / kinase binding / disordered domain specific binding / endocytic vesicle membrane / synaptic vesicle / Cargo recognition for clathrin-mediated endocytosis / presynapse / Clathrin-mediated endocytosis / protein-containing complex assembly / cytoplasmic vesicle / Potential therapeutics for SARS / transmembrane transporter binding / postsynapse / protein domain specific binding / synapse / lipid binding / protein-containing complex binding / protein kinase binding / glutamatergic synapse / membrane / plasma membrane / cytosol
Similarity search - Function
AP-2 complex subunit sigma / Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain / Adaptor protein complex AP-2, alpha subunit / Alpha adaptin AP2, C-terminal domain / Mu2, C-terminal domain / AP-2 complex subunit mu, N-terminal / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain / AP-1/2/4 complex subunit beta / Adaptor protein complex, sigma subunit ...AP-2 complex subunit sigma / Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain / Adaptor protein complex AP-2, alpha subunit / Alpha adaptin AP2, C-terminal domain / Mu2, C-terminal domain / AP-2 complex subunit mu, N-terminal / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain / AP-1/2/4 complex subunit beta / Adaptor protein complex, sigma subunit / : / Beta-adaptin appendage, C-terminal subdomain / Beta2-adaptin appendage, C-terminal sub-domain / AP complex subunit beta / Clathrin adaptor complex, small chain / Clathrin adaptor complexes small chain signature. / Clathrin adaptor complexes medium chain signature 1. / Clathrin adaptor, mu subunit / Clathrin adaptor, mu subunit, conserved site / Clathrin adaptor complexes medium chain signature 2. / : / Coatomer/calthrin adaptor appendage, C-terminal subdomain / Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain / Adaptin C-terminal domain / Adaptin C-terminal domain / AP complex, mu/sigma subunit / Clathrin adaptor complex small chain / Adaptor complexes medium subunit family / AP-2 complex subunit mu, C-terminal superfamily / Clathrin/coatomer adaptor, adaptin-like, N-terminal / Adaptin N terminal region / Mu homology domain / Mu homology domain (MHD) profile. / Clathrin adaptor, appendage, Ig-like subdomain superfamily / Longin-like domain superfamily / TBP domain superfamily / Armadillo/beta-catenin-like repeats / Armadillo / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
AP-2 complex subunit alpha-2 / AP-2 complex subunit sigma / AP-2 complex subunit beta / AP-2 complex subunit mu
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat) / Homo sapiens (human) / Mus musculus (house mouse)
Methodsubtomogram averaging / cryo EM / Resolution: 10.2 Å
AuthorsKovtun O / Kane Dickson V
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Wellcome Trust207455/Z/17/Z United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UP_1201/16 United Kingdom
CitationJournal: Sci Adv / Year: 2020
Title: Architecture of the AP2/clathrin coat on the membranes of clathrin-coated vesicles.
Authors: Oleksiy Kovtun / Veronica Kane Dickson / Bernard T Kelly / David J Owen / John A G Briggs /
Abstract: Clathrin-mediated endocytosis (CME) is crucial for modulating the protein composition of a cell's plasma membrane. Clathrin forms a cage-like, polyhedral outer scaffold around a vesicle, to which ...Clathrin-mediated endocytosis (CME) is crucial for modulating the protein composition of a cell's plasma membrane. Clathrin forms a cage-like, polyhedral outer scaffold around a vesicle, to which cargo-selecting clathrin adaptors are attached. Adaptor protein complex (AP2) is the key adaptor in CME. Crystallography has shown AP2 to adopt a range of conformations. Here, we used cryo-electron microscopy, tomography, and subtomogram averaging to determine structures, interactions, and arrangements of clathrin and AP2 at the key steps of coat assembly, from AP2 in solution to membrane-assembled clathrin-coated vesicles (CCVs). AP2 binds cargo and PtdIns(4,5) (phosphatidylinositol 4,5-bisphosphate)-containing membranes via multiple interfaces, undergoing conformational rearrangement from its cytosolic state. The binding mode of AP2 β2 appendage into the clathrin lattice in CCVs and buds implies how the adaptor structurally modulates coat curvature and coat disassembly.
History
DepositionMar 12, 2020-
Header (metadata) releaseJul 29, 2020-
Map releaseJul 29, 2020-
UpdateMay 22, 2024-
Current statusMay 22, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.3
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  • Surface view with fitted model
  • Atomic models: PDB-6yah
  • Surface level: 0.3
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6yah
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10751.png

Downloads & links

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Map

FileDownload / File: emd_10751.map.gz / Format: CCP4 / Size: 6.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map of AP2 in clathrin coat formed on membranes containing dileucine- and tyrosine-based cargo peptides
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.79 Å/pix.
x 120 pix.
= 214.44 Å		1.79 Å/pix.
x 120 pix.
= 214.44 Å		1.79 Å/pix.
x 120 pix.
= 214.44 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.787 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.3 / Movie #1: 0.3
Minimum - Maximum-2.3564742 - 2.5479515
Average (Standard dev.)-0.00039217158 (±0.21370192)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions120120120
Spacing120120120
CellA=B=C: 214.43999 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.7871.7871.787
M x/y/z120120120
origin x/y/z0.0000.0000.000
length x/y/z214.440214.440214.440
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS120120120
D min/max/mean-2.3562.548-0.000

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Supplemental data

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Mask #1

Fileemd_10751_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unsharpened half-map of AP2 in clathrin coat formed...

Fileemd_10751_half_map_1.map
AnnotationUnsharpened half-map of AP2 in clathrin coat formed on membranes containing dileucine- and tyrosine-based cargo peptides
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unsharpened half-map of AP2 in clathrin coat formed...

Fileemd_10751_half_map_2.map
AnnotationUnsharpened half-map of AP2 in clathrin coat formed on membranes containing dileucine- and tyrosine-based cargo peptides
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Clathrin/AP2 coat assembled on AP2 membrane.

EntireName: Clathrin/AP2 coat assembled on AP2 membrane.
Components
  • Complex: Clathrin/AP2 coat assembled on AP2 membrane.
    • Complex: AP-2 complex in clathrin coat, subunits alpha-2 and mu
      • Protein or peptide: AP-2 complex subunit alpha-2
      • Protein or peptide: AP-2 complex subunit mu
    • Complex: AP-2 complex in clathrin coat, subunit beta
      • Protein or peptide: AP-2 complex subunit beta
    • Complex: AP-2 complex in clathrin coat, subunit sigma
      • Protein or peptide: AP-2 complex subunit sigma

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Supramolecule #1: Clathrin/AP2 coat assembled on AP2 membrane.

SupramoleculeName: Clathrin/AP2 coat assembled on AP2 membrane. / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Clathrin/AP coat was formed on the membrane containing dileucine- and tyrosine-based cargo signal peptides. The AP2 adaptor lacked hinge and appendage regions in its alpha subunit.

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Supramolecule #2: AP-2 complex in clathrin coat, subunits alpha-2 and mu

SupramoleculeName: AP-2 complex in clathrin coat, subunits alpha-2 and mu
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1, #3
Details: AP2 in clathrin coat formed on membranes containing dileucine- and tyrosine-based cargo peptides
Source (natural)Organism: Rattus norvegicus (Norway rat)

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Supramolecule #3: AP-2 complex in clathrin coat, subunit beta

SupramoleculeName: AP-2 complex in clathrin coat, subunit beta / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Details: AP2 in clathrin coat formed on membranes containing dileucine- and tyrosine-based cargo peptides
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: AP-2 complex in clathrin coat, subunit sigma

SupramoleculeName: AP-2 complex in clathrin coat, subunit sigma / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #4
Details: AP2 in clathrin coat formed on membranes containing dileucine- and tyrosine-based cargo peptides
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: AP-2 complex subunit alpha-2

MacromoleculeName: AP-2 complex subunit alpha-2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 70.310062 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC KLLFIFLLGH DIDFGHMEAV NLLSSNRYT EKQIGYLFIS VLVNSNSELI RLINNAIKND LASRNPTFMG LALHCIANVG SREMAEAFAG EIPKILVAGD T MDSVKQSA ...String:
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC KLLFIFLLGH DIDFGHMEAV NLLSSNRYT EKQIGYLFIS VLVNSNSELI RLINNAIKND LASRNPTFMG LALHCIANVG SREMAEAFAG EIPKILVAGD T MDSVKQSA ALCLLRLYRT SPDLVPMGDW TSRVVHLLND QHLGVVTAAT SLITTLAQKN PEEFKTSVSL AVSRLSRIVT SA STDLQDY TYYFVPAPWL SVKLLRLLQC YPPPEDPAVR GRLTECLETI LNKAQEPPKS KKVQHSNAKN AVLFEAISLI IHH DSEPNL LVRACNQLGQ FLQHRETNLR YLALESMCTL ASSEFSHEAV KTHIETVINA LKTERDVSVR QRAVDLLYAM CDRS NAQQI VAEMLSYLET ADYSIREEIV LKVAILAEKY AVDYTWYVDT ILNLIRIAGD YVSEEVWYRV IQIVINRDDV QGYAA KTVF EALQAPACHE NLVKVGGYIL GEFGNLIAGD PRSSPLIQFN LLHSKFHLCS VPTRALLLST YIKFVNLFPE VKATIQ DVL RSDSQLKNAD VELQQRAVEY LRLSTVASTD ILATVLEEMP PFPERESSIL AKLKKKKGGS GLVPR

UniProtKB: AP-2 complex subunit alpha-2

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Macromolecule #2: AP-2 complex subunit beta

MacromoleculeName: AP-2 complex subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 105.619344 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHMTD SKYFTTNKKG EIFELKAELN NEKKEKRKEA VKKVIAAMTV GKDVSSLFPD VVNCMQTDNL ELKKLVYLYL MNYAKSQPD MAIMAVNSFV KDCEDPNPLI RALAVRTMGC IRVDKITEYL CEPLRKCLKD EDPYVRKTAA VCVAKLHDIN A QMVEDQGF ...String:
MHHHHHHMTD SKYFTTNKKG EIFELKAELN NEKKEKRKEA VKKVIAAMTV GKDVSSLFPD VVNCMQTDNL ELKKLVYLYL MNYAKSQPD MAIMAVNSFV KDCEDPNPLI RALAVRTMGC IRVDKITEYL CEPLRKCLKD EDPYVRKTAA VCVAKLHDIN A QMVEDQGF LDSLRDLIAD SNPMVVANAV AALSEISESH PNSNLLDLNP QNINKLLTAL NECTEWGQIF ILDCLSNYNP KD DREAQSI CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY VALRNINLIV QKR PEILKQ EIKVFFVKYN DPIYVKLEKL DIMIRLASQA NIAQVLAELK EYATEVDVDF VRKAVRAIGR CAIKVEQSAE RCVS TLLDL IQTKVNYVVQ EAIVVIRDIF RKYPNKYESI IATLCENLDS LDEPDARAAM IWIVGEYAER IDNADELLES FLEGF HDES TQVQLTLLTA IVKLFLKKPS ETQELVQQVL SLATQDSDNP DLRDRGYIYW RLLSTDPVTA KEVVLSEKPL ISEETD LIE PTLLDELICH IGSLASVYHK PPNAFVEGSH GIHRKHLPIH HGSTDAGDSP VGTTTATNLE QPQVIPSQGD LLGDLLN LD LGPPVNVPQV SSMQMGAVDL LGGGLDSLVG QSFIPSSVPA TFAPSPTPAV VSSGLNDLFE LSTGIGMAPG GYVAPKAV W LPAVKAKGLE ISGTFTHRQG HIYMEMNFTN KALQHMTDFA IQFNKNSFGV IPSTPLAIHT PLMPNQSIDV SLPLNTLGP VMKMEPLNNL QVAVKNNIDV FYFSCLIPLN VLFVEDGKME RQVFLATWKD IPNENELQFQ IKECHLNADT VSSKLQNNNV YTIAKRNVE GQDMLYQSLK LTNGIWILAE LRIQPGNPNY TLSLKCRAPE VSQYIYQVYD SILKN

UniProtKB: AP-2 complex subunit beta

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Macromolecule #3: AP-2 complex subunit mu

MacromoleculeName: AP-2 complex subunit mu / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 51.044113 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR SNIWLAAVTK QNVNAAMVFE FLYKMCDVM AAYFGKISEE NIKNNFVLIY ELLDEILDFG YPQNSETGAL KTFITQQGIK SQHQTKEEQS QITSQVTGQI G WRREGIKY ...String:
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR SNIWLAAVTK QNVNAAMVFE FLYKMCDVM AAYFGKISEE NIKNNFVLIY ELLDEILDFG YPQNSETGAL KTFITQQGIK SQHQTKEEQS QITSQVTGQI G WRREGIKY RRNELFLDVL ESVNLLMSPQ GQVLSAHVSG RVVMKSYLSG MPECKFGMND KIVIEKQGKG TADETSKSME QK LISEEDL GKQSIAIDDC TFHQCVRLSK FDSERSISFI PPDGEFELMR YRTTKDIILP FRVIPLVREV GRTKLEVKVV IKS NFKPSL LAQKIEVRIP TPLNTSGVQV ICMKGKAKYK ASENAIVWKI KRMAGMKESQ ISAEIELLPT NDKKKWARPP ISMN FEVPF APSGLKVRYL KVFEPKLNYS DHDVIKWVRY IGRSGIYETR C

UniProtKB: AP-2 complex subunit mu

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Macromolecule #4: AP-2 complex subunit sigma

MacromoleculeName: AP-2 complex subunit sigma / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 17.038688 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MIRFILIQNR AGKTRLAKWY MQFDDDEKQK LIEEVHAVVT VRDAKHTNFV EFRNFKIIYR RYAGLYFCIC VDVNDNNLAY LEAIHNFVE VLNEYFHNVC ELDLVFNFYK VYTVVDEMFL AGEIRETSQT KVLKQLLMLQ SLE

UniProtKB: AP-2 complex subunit sigma

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Experimental details

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Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation state3D array

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Sample preparation

Concentration0.7 mg/mL
BufferpH: 7.2
Component:
ConcentrationName
10.0 mMHepes KOH
120.0 mMPotassium Acetate
2.0 mMMagnesium chloride
5.0 mM2-Mercaptoethanol
GridModel: C-flat-2/2 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 98 % / Chamber temperature: 291 K / Instrument: LEICA EM GP
Details: The sample was supplemented with 10 nm nanogold fiducials, and 3 ul of the mixture was backside blotted for 3 seconds..
DetailsThe sample (in vitro budding reaction) contained AP2, clathrin and 400 nm extruded liposomes

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Digitization - Frames/image: 1-10 / Number grids imaged: 2 / Average exposure time: 0.2 sec. / Average electron dose: 3.2 e/Å2
Details: The images were collected in movie mode at 10 frames per second
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Calibrated defocus max: 6.5 µm / Calibrated defocus min: 1.5 µm / Calibrated magnification: 81000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 6.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 81000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

DetailsThe images were low pass filtered according to the cumulative radiation dose.
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 10.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software: (Name: TOM, AV3) / Number subtomograms used: 27630
ExtractionNumber tomograms: 29139 / Number images used: 292224 / Reference model: reference-free
Method: geometrically defined initial positions on membrane strctures
Final 3D classificationSoftware: (Name: PEET, Dynamo)
Final angle assignmentType: OTHER / Software: (Name: TOM, AV3)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

1xa7


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT / Target criteria: correlation coefficient
Output model

PDB-6yah:
AP2 in clathrin coats assembled on a membrane containing dileucine- and tyrosine-based cargo peptides

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