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- EMDB-60208: Structure of Polycystin-1/Polycystin-2 complex with GOF mutations -

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Basic information

Entry
Database: EMDB / ID: EMD-60208
TitleStructure of Polycystin-1/Polycystin-2 complex with GOF mutations
Map data
Sample
  • Complex: Structure of Polycystin-1/Polycystin-2 complex with GOF mutations
    • Protein or peptide: Polycystin-1
    • Protein or peptide: Polycystin-2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
Keywordsion channel / MEMBRANE PROTEIN
Function / homology
Function and homology information


metanephric distal tubule morphogenesis / nitrogen cycle metabolic process / detection of nodal flow / metanephric smooth muscle tissue development / metanephric cortex development / metanephric cortical collecting duct development / metanephric distal tubule development / polycystin complex / mesonephric tubule development / mesonephric duct development ...metanephric distal tubule morphogenesis / nitrogen cycle metabolic process / detection of nodal flow / metanephric smooth muscle tissue development / metanephric cortex development / metanephric cortical collecting duct development / metanephric distal tubule development / polycystin complex / mesonephric tubule development / mesonephric duct development / metanephric part of ureteric bud development / renal tubule morphogenesis / determination of liver left/right asymmetry / lung epithelium development / metanephric ascending thin limb development / lymph vessel morphogenesis / metanephric mesenchyme development / metanephric S-shaped body morphogenesis / basal cortex / renal artery morphogenesis / mitocytosis / metanephric proximal tubule development / HLH domain binding / calcium-induced calcium release activity / calcium-independent cell-matrix adhesion / Wnt receptor activity / migrasome / cilium organization / genitalia development / VxPx cargo-targeting to cilium / detection of mechanical stimulus / muscle alpha-actinin binding / regulation of calcium ion import / voltage-gated monoatomic ion channel activity / placenta blood vessel development / cellular response to hydrostatic pressure / Golgi-associated vesicle membrane / response to fluid shear stress / cellular response to fluid shear stress / metanephric collecting duct development / cation channel complex / outward rectifier potassium channel activity / cartilage development / non-motile cilium / actinin binding / cellular response to osmotic stress / determination of left/right symmetry / digestive tract development / : / voltage-gated monoatomic cation channel activity / neural tube development / voltage-gated sodium channel activity / aorta development / motile cilium / ciliary membrane / branching involved in ureteric bud morphogenesis / cartilage condensation / skin development / protein heterotetramerization / negative regulation of G1/S transition of mitotic cell cycle / branching morphogenesis of an epithelial tube / spinal cord development / heart looping / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / establishment of cell polarity / cytoplasmic side of endoplasmic reticulum membrane / homophilic cell-cell adhesion / centrosome duplication / regulation of G1/S transition of mitotic cell cycle / lateral plasma membrane / anatomical structure morphogenesis / voltage-gated potassium channel activity / cell surface receptor signaling pathway via JAK-STAT / potassium channel activity / embryonic placenta development / regulation of cell adhesion / monoatomic cation channel activity / voltage-gated calcium channel activity / transcription regulator inhibitor activity / cytoskeletal protein binding / regulation of proteasomal protein catabolic process / release of sequestered calcium ion into cytosol / potassium ion transmembrane transport / calcium channel complex / sodium ion transmembrane transport / cellular response to calcium ion / protein export from nucleus / basal plasma membrane / cytoplasmic vesicle membrane / regulation of mitotic spindle organization / cellular response to cAMP / cell-matrix adhesion / lumenal side of endoplasmic reticulum membrane / cellular response to reactive oxygen species / protein tetramerization / kidney development / phosphoprotein binding / establishment of localization in cell / liver development / peptidyl-serine phosphorylation
Similarity search - Function
Polycystic kidney disease type 1 protein / PKD/REJ-like domain / Polycystin cation channel / REJ domain / REJ domain / REJ domain profile. / Polycystin-1 like, PLAT/LH2 domain / Carbohydrate-binding WSC / WSC domain / WSC domain profile. ...Polycystic kidney disease type 1 protein / PKD/REJ-like domain / Polycystin cation channel / REJ domain / REJ domain / REJ domain profile. / Polycystin-1 like, PLAT/LH2 domain / Carbohydrate-binding WSC / WSC domain / WSC domain profile. / present in yeast cell wall integrity and stress response component proteins / PKD domain / Ferredoxin I 4Fe-4S cluster domain / : / Polycystic kidney disease type 2 protein / Polycystin domain / Polycystin domain / Lipoxygenase homology 2 (beta barrel) domain / PLAT/LH2 domain / PLAT/LH2 domain superfamily / PLAT/LH2 domain / PLAT domain profile. / Polycystic kidney disease (PKD) domain profile. / : / GPS motif / GAIN-B domain profile. / G-protein-coupled receptor proteolytic site domain / PKD domain / Polycystin cation channel, PKD1/PKD2 / Polycystin cation channel / PKD domain superfamily / PKD/Chitinase domain / Repeats in polycystic kidney disease 1 (PKD1) and other proteins / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like / C-type lectin (CTL) or carbohydrate-recognition domain (CRD) / C-type lectin-like/link domain superfamily / C-type lectin fold / Voltage-dependent channel domain superfamily / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Immunoglobulin-like fold
Similarity search - Domain/homology
Polycystin-1 / Polycystin-2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / Resolution: 3.34 Å
AuthorsChen MY / Su Q / Shi YG / Yu Y
Funding support China, 2 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31930059 China
National Natural Science Foundation of China (NSFC)81970633 China
CitationJournal: To Be Published
Title: Structure of Polycystin-1/Polycystin-2 complex with GOF mutations
Authors: Chen MY / Su Q / Shi YG
History
DepositionMay 17, 2024-
Header (metadata) releaseMay 21, 2025-
Map releaseMay 21, 2025-
UpdateJul 23, 2025-
Current statusJul 23, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_60208.png

Downloads & links

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Map

FileDownload / File: emd_60208.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 240 pix.
= 260.88 Å		1.09 Å/pix.
x 240 pix.
= 260.88 Å		1.09 Å/pix.
x 240 pix.
= 260.88 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.087 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.019
Minimum - Maximum-0.0957849 - 0.17356876
Average (Standard dev.)0.0003851044 (±0.005440991)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 260.88 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_60208_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_60208_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Structure of Polycystin-1/Polycystin-2 complex with GOF mutations

EntireName: Structure of Polycystin-1/Polycystin-2 complex with GOF mutations
Components
  • Complex: Structure of Polycystin-1/Polycystin-2 complex with GOF mutations
    • Protein or peptide: Polycystin-1
    • Protein or peptide: Polycystin-2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Structure of Polycystin-1/Polycystin-2 complex with GOF mutations

SupramoleculeName: Structure of Polycystin-1/Polycystin-2 complex with GOF mutations
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Polycystin-1

MacromoleculeName: Polycystin-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 138.514672 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDYKDDDDKG ASLFVPPSHV RFVFPEPTAD VNYIVMLTCA VCLVTYMVMA AILHKLDQLD ASRGRAIPFC GQRGRFKYEI LVKTGWGRG SGTTAHVGIM LYGVDSRSGH RHLDGDRAFH RNSLDIFRIA TPHSLGSVWK IRVWHDNKGL SPAWFLQHVI V RDLQTARS ...String:
MDYKDDDDKG ASLFVPPSHV RFVFPEPTAD VNYIVMLTCA VCLVTYMVMA AILHKLDQLD ASRGRAIPFC GQRGRFKYEI LVKTGWGRG SGTTAHVGIM LYGVDSRSGH RHLDGDRAFH RNSLDIFRIA TPHSLGSVWK IRVWHDNKGL SPAWFLQHVI V RDLQTARS AFFLVNDWLS VETEANGGLV EKEVLAASDA ALLRFRRLLV AELQRGFFDK HIWLSIWDRP PRSRFTRIQR AT CCVLLIC LFLGANAVWY GAVGDSAYST GHVSRLSPLS VDTVAVGLVS SVVVYPVYLA ILFLFRMSRS KVAGSPSPTP AGQ QVLDID SCLDSSVLDS SFLTFSGLHA EQAFVGQMKS DLFLDDSKSL VCWPSGEGTL SWPDLLSDPS IVGSNLRQLA RGQA GHGLG PEEDGFSLAS PYSPAKSFSA SDEDLIQQVL AEGVSSPAPT QDTHMETDLL SSLSSTPGEK TETLALQRLG ELGPP SPGL NWEQPQAARL SRTGLVEGLR KRLLPAWCAS LAHGLSLLLV AVAVAVSGWV GASFPPGVSV AWLLSSSASF LASFLG WEP LKVLLEALYF SLVAKRLHPD EDDTLVESPA VTPVSARVPR VRPPHGFALF LAKEEARKVK RLHGMLRSLL VYMLFLL VT LLASYGDASC HGHAYRLQSA IKQELHSRAF LAITRSEELW PWMAHVLLPY VHGNQSSPEL GPPRLRQVRL QEALYPDP P GPRVHTCSAA GGFSTSDYDV GWESPHNGSG TWAYSAPDLL GAWSWGSCAV YDSGGYVQEL GLSLEESRDR LRFLQLHNW LDNRSRAVFL ELTRYSPAVG LHAAVTLRLE FPAAGRALAA LSVRPFALRR LSAGLSLPLL TSVCLLLFAV HFAVAEARTW HREGRWRVL RLGAWARWLL VALTAATALV RLAQLGAADR QWTRFVRGRP RRFTSFDQVA QLSSAARGLA ASLLFLLLVK A AQQLRFVR QWSVFGKTLC RALPELLGVT LGLVVLGVAY AQLAILLVSS CVDSLWSVAQ ALLVLCPGTG LSTLCPAESW HL SPLLCVG LWALRLWGAL RLGAVILRWR YHALRGELYR PAWEPQDYEM VELFLRRLRL WMGLSKVKEF RHKVRFEGME PLP SRSSRG SKVSPDVPPP SAGSDASHPS TSSSQLDGLS VSLGRLGTRC EPEPSRLQAV FEALLTQFDR LNQATEDVYQ LEQQ LHSLQ GRRSSRAPAG SSRGPSPGLR PALPSRLARA SRGVDLATGP SRTPLRAKNK VHPSST

UniProtKB: Polycystin-1

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Macromolecule #2: Polycystin-2

MacromoleculeName: Polycystin-2 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 113.555008 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGASSAWSHP QFEKGGGSGG GSGGSAWSHP QFEKGSAAAM VNSSRVQPQQ PGDAKRPPAP RAPDPGRLMA GCAAVGASLA APGGLCEQR GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP G SRRSAASS ...String:
MGASSAWSHP QFEKGGGSGG GSGGSAWSHP QFEKGSAAAM VNSSRVQPQQ PGDAKRPPAP RAPDPGRLMA GCAAVGASLA APGGLCEQR GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP G SRRSAASS AVSSVGARSR GLGGYHGAGH PSGRRRRRED QGPPCPSPVG GGDPLHRHLP LEGQPPRVAW AERLVRGLRG LW GTRLMEE SSTNREKYLK SVLRELVTYL LFLIVLCILT YGMMSSNVYY YTRMMSQLFL DTPVSKTEKT NFKTLSSMED FWK FTEGSL LDGLYWKMQP SNQTEADNRS FIFYENLLLG VPRIRQLRVR NGSCSIPQDL RDEIKECYDV YSVSSEDRAP FGPR NGTAW IYTSEKDLNG SSHWGIIATY SGAGYYLDLS RTREETAAQV ASLKKNVWLD RGTRATFIDF SVYNANINLF CVVRL LVEF PATGGVIPSW QFQPLKLIRY VTTFDFFLAA CEIIFCFFIF YYVVEEILEI RIHKLHYFRS FWNCLDVVIV VLSVVA IGI NIYRTSNVEV LLQFLEDQNT FPNFEHLAYW QIQFNNIAAV TVFFVWIKLF KFINFNRTMS QLSTTMSRCA KDLFGFA IM FFIIFLAYAQ LAYLVFGTQV DDFSTFQECI FTQFRIILGD INFAEIEEAN RVLGPIYFTT FVFFMFFILL NMFLAIIN D TYSEVKSDLA QQKAEMELSD LIRKGYHKAL VKLKLKKNTV DDISESLRQG GGKLNFDELR QDLKGKGHTD AEIEAIFTK YDQDGDQELT EHEHQQMRDD LEKEREDLDL DHSSLPRPMS SRSFPRSLDD SEEDDDEDSG HSSRRRGSIS SGVSYEEFQV LVRRVDRME HSIGSIVSKI DAVIVKLEIM ERAKLKRREV LGRLLDGVAE DERLGRDSEI HREQMERLVR EELERWESDD A ASQISHGL GTPVGLNGQP RPRSSRPSSS QSTEGMEGAG GNGSSNVHV

UniProtKB: Polycystin-2

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Macromolecule #3: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 3 / Number of copies: 9 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

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

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Experimental details

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Structure determination

Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4

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Electron microscopy

MicroscopeFEI POLARA 300
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6d1w

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.34 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 276741
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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