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- EMDB-45655: Cryo-EM structure of alpha5beta1 integrin in complex with NeoNectin -

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Basic information

Entry
Database: EMDB / ID: EMD-45655
TitleCryo-EM structure of alpha5beta1 integrin in complex with NeoNectin
Map dataSharpened map 3.19Angstrom
Sample
  • Complex: Protein complex of wild type integrin alpha-5 beta-1 with computationally designed protein NeoNectin
    • Protein or peptide: Integrin alpha-5
    • Protein or peptide: Integrin beta-1
    • Protein or peptide: NeoNectin
  • Ligand: CALCIUM ION
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: MANGANESE (II) ION
Keywordsa5B1 / de novo / tissue regeneration / extracellular matrix protein / SIGNALING PROTEIN
Function / homology
Function and homology information


integrin alpha8-beta1 complex / integrin alpha3-beta1 complex / integrin alpha5-beta1 complex / integrin alpha7-beta1 complex / integrin alpha10-beta1 complex / integrin alpha11-beta1 complex / positive regulation of glutamate uptake involved in transmission of nerve impulse / myoblast fate specification / regulation of inward rectifier potassium channel activity / regulation of collagen catabolic process ...integrin alpha8-beta1 complex / integrin alpha3-beta1 complex / integrin alpha5-beta1 complex / integrin alpha7-beta1 complex / integrin alpha10-beta1 complex / integrin alpha11-beta1 complex / positive regulation of glutamate uptake involved in transmission of nerve impulse / myoblast fate specification / regulation of inward rectifier potassium channel activity / regulation of collagen catabolic process / integrin alpha9-beta1 complex / integrin alpha4-beta1 complex / cell-cell adhesion mediated by integrin / C-X3-C chemokine binding / cardiac cell fate specification / integrin binding involved in cell-matrix adhesion / integrin alpha1-beta1 complex / collagen binding involved in cell-matrix adhesion / integrin alpha2-beta1 complex / Localization of the PINCH-ILK-PARVIN complex to focal adhesions / regulation of synapse pruning / reactive gliosis / formation of radial glial scaffolds / cerebellar climbing fiber to Purkinje cell synapse / Other semaphorin interactions / Formation of the ureteric bud / CD40 signaling pathway / positive regulation of vascular endothelial growth factor signaling pathway / calcium-independent cell-matrix adhesion / integrin alphav-beta1 complex / positive regulation of fibroblast growth factor receptor signaling pathway / Fibronectin matrix formation / basement membrane organization / myelin sheath abaxonal region / alphav-beta3 integrin-vitronectin complex / CHL1 interactions / cardiac muscle cell myoblast differentiation / Laminin interactions / RUNX2 regulates genes involved in cell migration / MET interacts with TNS proteins / germ cell migration / leukocyte tethering or rolling / cardiac muscle cell differentiation / cell projection organization / Platelet Adhesion to exposed collagen / vascular endothelial growth factor receptor 2 binding / myoblast fusion / Elastic fibre formation / mesodermal cell differentiation / cell-substrate junction assembly / platelet-derived growth factor receptor binding / axon extension / positive regulation of fibroblast migration / positive regulation of vascular endothelial growth factor receptor signaling pathway / cell migration involved in sprouting angiogenesis / wound healing, spreading of epidermal cells / regulation of spontaneous synaptic transmission / heterotypic cell-cell adhesion / myoblast differentiation / integrin complex / positive regulation of cell-substrate adhesion / dendrite morphogenesis / Basigin interactions / Molecules associated with elastic fibres / muscle organ development / negative regulation of Rho protein signal transduction / lamellipodium assembly / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / MET activates PTK2 signaling / cell adhesion mediated by integrin / negative regulation of vasoconstriction / leukocyte cell-cell adhesion / Syndecan interactions / epidermal growth factor receptor binding / positive regulation of wound healing / maintenance of blood-brain barrier / sarcomere organization / positive regulation of neuroblast proliferation / cell-substrate adhesion / positive regulation of sprouting angiogenesis / endodermal cell differentiation / TGF-beta receptor signaling activates SMADs / homophilic cell adhesion via plasma membrane adhesion molecules / establishment of mitotic spindle orientation / glial cell projection / cleavage furrow / fibronectin binding / cellular response to low-density lipoprotein particle stimulus / negative regulation of anoikis / intercalated disc / RHOG GTPase cycle / negative regulation of neuron differentiation / ECM proteoglycans / neuroblast proliferation / RAC2 GTPase cycle / RAC3 GTPase cycle / Integrin cell surface interactions / cellular defense response / coreceptor activity / phagocytosis
Similarity search - Function
Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : / Integrin alpha Ig-like domain 3 / Integrin beta tail domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily ...Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : / Integrin alpha Ig-like domain 3 / Integrin beta tail domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain cysteine-rich domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / EGF-like domain, extracellular / EGF-like domain / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / : / Integrin alpha Ig-like domain 2 / Integrin alpha chain / Integrin alpha beta-propellor / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / Integrins alpha chain signature. / FG-GAP repeat profile. / Integrin alpha (beta-propellor repeats). / FG-GAP repeat / FG-GAP repeat / Integrin alpha, N-terminal / Integrin domain superfamily / PSI domain / domain found in Plexins, Semaphorins and Integrins / von Willebrand factor A-like domain superfamily / EGF-like domain signature 1.
Similarity search - Domain/homology
Integrin beta-1 / Integrin alpha-5
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.19 Å
AuthorsWerther R / Nguyen A / Estrada Alamo KA / Wang X / Campbell MG
Funding support United States, 4 items
OrganizationGrant numberCountry
The Pew Charitable Trusts United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM147414-01 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)P30 CA015704-40; RRID:SCR_022611 United States
Other privateSeattle Cancer Consortium Safeway Inc Pilot Grant
CitationJournal: To Be Published
Title: De Novo Design of Integrin alpha5beta1 Modulating Proteins for Regenerative Medicine
Authors: Wang X / Guillem-Marti J / Kumar S / Lee DS / Cabrerizo-Aguado D / Werther R / Estrada Alamo KA / Zhao YT / Nguyen A / Kopyeva I / Huang B / Li J / Hao Y / Li X / Brizuela-Velasco A / Murray ...Authors: Wang X / Guillem-Marti J / Kumar S / Lee DS / Cabrerizo-Aguado D / Werther R / Estrada Alamo KA / Zhao YT / Nguyen A / Kopyeva I / Huang B / Li J / Hao Y / Li X / Brizuela-Velasco A / Murray AN / Gerben S / Roy A / DeForest CA / Springer T / Ruohola-Baker H / Cooper JA / Campbell MG / Maria Manero J / Ginebra M / Baker D
History
DepositionJul 9, 2024-
Header (metadata) releaseJul 17, 2024-
Map releaseJul 17, 2024-
UpdateJul 17, 2024-
Current statusJul 17, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45655.png

Downloads & links

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Map

FileDownload / File: emd_45655.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map 3.19Angstrom
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.12 Å/pix.
x 352 pix.
= 394.944 Å		1.12 Å/pix.
x 352 pix.
= 394.944 Å		1.12 Å/pix.
x 352 pix.
= 394.944 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.122 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.24
Minimum - Maximum-1.0254947 - 2.0571992
Average (Standard dev.)0.000040452403 (±0.033777367)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions352352352
Spacing352352352
CellA=B=C: 394.944 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_45655_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Additional unsharpened map 3.19Angstrom

Fileemd_45655_additional_1.map
AnnotationAdditional unsharpened map 3.19Angstrom
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Additional sharpened map 3.28Angstrom

Fileemd_45655_additional_2.map
AnnotationAdditional sharpened map 3.28Angstrom
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

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Additional map: Additional unsharpened map 3.28Angstrom

Fileemd_45655_additional_3.map
AnnotationAdditional unsharpened map 3.28Angstrom
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map B from 3.19Angstrom map

Fileemd_45655_half_map_1.map
AnnotationHalf Map B from 3.19Angstrom map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map A from 3.19Angstrom map

Fileemd_45655_half_map_2.map
AnnotationHalf Map A from 3.19Angstrom map
Projections & Slices
AxesZYX

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Sample components

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Entire : Protein complex of wild type integrin alpha-5 beta-1 with computa...

EntireName: Protein complex of wild type integrin alpha-5 beta-1 with computationally designed protein NeoNectin
Components
  • Complex: Protein complex of wild type integrin alpha-5 beta-1 with computationally designed protein NeoNectin
    • Protein or peptide: Integrin alpha-5
    • Protein or peptide: Integrin beta-1
    • Protein or peptide: NeoNectin
  • Ligand: CALCIUM ION
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: MANGANESE (II) ION

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Supramolecule #1: Protein complex of wild type integrin alpha-5 beta-1 with computa...

SupramoleculeName: Protein complex of wild type integrin alpha-5 beta-1 with computationally designed protein NeoNectin
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Integrin alpha-5

MacromoleculeName: Integrin alpha-5 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 109.695867 KDa
Recombinant expressionOrganism: Cricetulus griseus (Chinese hamster)
SequenceString: MGSRTPESPL HAVQLRWGPR RRPPLLPLLL LLLPPPPRVG GFNLDAEAPA VLSGPPGSFF GFSVEFYRPG TDGVSVLVGA PKANTSQPG VLQGGAVYLC PWGASPTQCT PIEFDSKGSR LLESSLSSSE GEEPVEYKSL QWFGATVRAH GSSILACAPL Y SWRTEKEP ...String:
MGSRTPESPL HAVQLRWGPR RRPPLLPLLL LLLPPPPRVG GFNLDAEAPA VLSGPPGSFF GFSVEFYRPG TDGVSVLVGA PKANTSQPG VLQGGAVYLC PWGASPTQCT PIEFDSKGSR LLESSLSSSE GEEPVEYKSL QWFGATVRAH GSSILACAPL Y SWRTEKEP LSDPVGTCYL STDNFTRILE YAPCRSDFSW AAGQGYCQGG FSAEFTKTGR VVLGGPGSYF WQGQILSATQ EQ IAESYYP EYLINLVQGQ LQTRQASSIY DDSYLGYSVA VGEFSGDDTE DFVAGVPKGN LTYGYVTILN GSDIRSLYNF SGE QMASYF GYAVAATDVN GDGLDDLLVG APLLMDRTPD GRPQEVGRVY VYLQHPAGIE PTPTLTLTGH DEFGRFGSSL TPLG DLDQD GYNDVAIGAP FGGETQQGVV FVFPGGPGGL GSKPSQVLQP LWAASHTPDF FGSALRGGRD LDGNGYPDLI VGSFG VDKA VVYRGRPIVS ASASLTIFPA MFNPEERSCS LEGNPVACIN LSFCLNASGK HVADSIGFTV ELQLDWQKQK GGVRRA LFL ASRQATLTQT LLIQNGARED CREMKIYLRN ESEFRDKLSP IHIALNFSLD PQAPVDSHGL RPALHYQSKS RIEDKAQ IL LDCGEDNICV PDLQLEVFGE QNHVYLGDKN ALNLTFHAQN VGEGGAYEAE LRVTAPPEAE YSGLVRHPGN FSSLSCDY F AVNQSRLLVC DLGNPMKAGA SLWGGLRFTV PHLRDTKKTI QFDFQILSKN LNNSQSDVVS FRLSVEAQAQ VTLNGVSKP EAVLFPVSDW HPRDQPQKEE DLGPAVHHVY ELINQGPSSI SQGVLELSCP QALEGQQLLY VTRVTGLNCT TNHPINPKGL ELDPEGSLH HQQKREAPSR SSASSGPQIL KCPEAECFRL RCELGPLHQQ ESQSLQLHFR VWAKTFLQRE HQPFSLQCEA V YKALKMPY RILPRQLPQK ERQVATAVQW TKAEGSYGTG GLEVLFQ

UniProtKB: Integrin alpha-5

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Macromolecule #2: Integrin beta-1

MacromoleculeName: Integrin beta-1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 81.743961 KDa
Recombinant expressionOrganism: Cricetulus griseus (Chinese hamster)
SequenceString: MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT SARCDDLEAL KKKGCPPDDI ENPRGSKDI KKNKNVTNRS KGTAEKLKPE DITQIQPQQL VLRLRSGEPQ TFTLKFKRAE DYPIDLYYLM DLSYSMKDDL E NVKSLGTD ...String:
MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT SARCDDLEAL KKKGCPPDDI ENPRGSKDI KKNKNVTNRS KGTAEKLKPE DITQIQPQQL VLRLRSGEPQ TFTLKFKRAE DYPIDLYYLM DLSYSMKDDL E NVKSLGTD LMNEMRRITS DFRIGFGSFV EKTVMPYIST TPAKLRNPCT SEQNCTSPFS YKNVLSLTNK GEVFNELVGK QR ISGNLDS PEGGFDAIMQ VAVCGSLIGW RNVTRLLVFS TDAGFHFAGD GKLGGIVLPN DGQCHLENNM YTMSHYYDYP SIA HLVQKL SENNIQTIFA VTEEFQPVYK ELKNLIPKSA VGTLSANSSN VIQLIIDAYN SLSSEVILEN GKLSEGVTIS YKSY CKNGV NGTGENGRKC SNISIGDEVQ FEISITSNKC PKKDSDSFKI RPLGFTEEVE VILQYICECE CQSEGIPESP KCHEG NGTF ECGACRCNEG RVGRHCECST DEVNSEDMDA YCRKENSSEI CSNNGECVCG QCVCRKRDNT NEIYSGKFCE CDNFNC DRS NGLICGGNGV CKCRVCECNP NYTGSACDCS LDTSTCEASN GQICNGRGIC ECGVCKCTDP KFQGQTCEMC QTCLGVC AE HKECVQCRAF NKGEKKDTCT QECSYFNITK VESRDKLPQP VQPDPVSHCK EKDVDDCWFY FTYSVNGNNE VMVHVVEN P ECPTGPDDTS GLEVLFQ

UniProtKB: Integrin beta-1

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Macromolecule #3: NeoNectin

MacromoleculeName: NeoNectin / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 11.270766 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGLNDIFEAQ KIEWHEGGSG GSELIIHGRG DFPSSELERL RERFERLGIK VRVDHKVLTL IGISEEEAER LARELRKRGI WVEIRKGGS LEHHHHHH

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Macromolecule #7: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 7 / Number of copies: 4 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #8: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 8 / Number of copies: 2 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #9: MANGANESE (II) ION

MacromoleculeName: MANGANESE (II) ION / type: ligand / ID: 9 / Number of copies: 3 / Formula: MN
Molecular weightTheoretical: 54.938 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.1 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
20.0 mMTrisTris
150.0 mMNaClsodium chloride
1.0 mMMnCl2manganese chloride
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 3 / Average electron dose: 50.0 e/Å2 / Details: Collection at 30 degrees tilt
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 36000
Sample stageCooling holder cryogen: NITROGEN

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.19 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 72604
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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