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Yorodumi- EMDB-32621: Cryo-EM structure of VWF D'D3 dimer (wild type) complexed with D1... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-32621 | |||||||||
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Title | Cryo-EM structure of VWF D'D3 dimer (wild type) complexed with D1D2 at 3.4 angstron resolution (1 unit) | |||||||||
Map data | ||||||||||
Sample |
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Keywords | blood / VWF / von Willebrand factor / von Willebrand disease / blood coagulation / blood clotting / multimer assembly / VWF assembly / D'D3 domain / D1D2 domain / D'D3 dimer / D1D2 Dimer / VWF Tube / repeating unit | |||||||||
Function / homology | Function and homology information Defective VWF binding to collagen type I / Enhanced cleavage of VWF variant by ADAMTS13 / Defective VWF cleavage by ADAMTS13 variant / Defective F8 binding to von Willebrand factor / Enhanced binding of GP1BA variant to VWF multimer:collagen / Defective binding of VWF variant to GPIb:IX:V / Weibel-Palade body / hemostasis / platelet alpha granule / Platelet Adhesion to exposed collagen ...Defective VWF binding to collagen type I / Enhanced cleavage of VWF variant by ADAMTS13 / Defective VWF cleavage by ADAMTS13 variant / Defective F8 binding to von Willebrand factor / Enhanced binding of GP1BA variant to VWF multimer:collagen / Defective binding of VWF variant to GPIb:IX:V / Weibel-Palade body / hemostasis / platelet alpha granule / Platelet Adhesion to exposed collagen / positive regulation of intracellular signal transduction / GP1b-IX-V activation signalling / p130Cas linkage to MAPK signaling for integrins / cell-substrate adhesion / Defective F8 cleavage by thrombin / Platelet Aggregation (Plug Formation) / immunoglobulin binding / GRB2:SOS provides linkage to MAPK signaling for Integrins / Integrin cell surface interactions / collagen binding / Intrinsic Pathway of Fibrin Clot Formation / Integrin signaling / extracellular matrix / platelet alpha granule lumen / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / platelet activation / response to wounding / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / blood coagulation / integrin binding / Platelet degranulation / protein-folding chaperone binding / protease binding / collagen-containing extracellular matrix / cell adhesion / endoplasmic reticulum / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Zeng JW / Shu ZM / Zhou AW | |||||||||
Funding support | China, 1 items
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Citation | Journal: Cell Discov / Year: 2022 Title: Structural mechanism of VWF D'D3 dimer formation. Authors: Zimei Shu / Jianwei Zeng / Li Xia / Haiyan Cai / Aiwu Zhou / | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_32621.map.gz | 2.9 MB | EMDB map data format | |
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Header (meta data) | emd-32621-v30.xml emd-32621.xml | 12.9 KB 12.9 KB | Display Display | EMDB header |
Images | emd_32621.png | 100.7 KB | ||
Filedesc metadata | emd-32621.cif.gz | 6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32621 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32621 | HTTPS FTP |
-Related structure data
Related structure data | 7wn4MC 7wn3C 7wn6C C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_32621.map.gz / Format: CCP4 / Size: 22.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.97 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : VWF D'D3-D1D2 complex (1 unit)
Entire | Name: VWF D'D3-D1D2 complex (1 unit) |
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Components |
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-Supramolecule #1: VWF D'D3-D1D2 complex (1 unit)
Supramolecule | Name: VWF D'D3-D1D2 complex (1 unit) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: von Willebrand antigen 2
Macromolecule | Name: von Willebrand antigen 2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 81.427703 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: AEGTRGRSST ARCSLFGSDF VNTFDGSMYS FAGYCSYLLA GGCQKRSFSI IGDFQNGKRV SLSVYLGEFF DIHLFVNGTV TQGDQRVSM PYASKGLYLE TEAGYYKLSG EAYGFVARID GSGNFQVLLS DRYFNKTCGL CGNFNIFAED DFMTQEGTLT S DPYDFANS ...String: AEGTRGRSST ARCSLFGSDF VNTFDGSMYS FAGYCSYLLA GGCQKRSFSI IGDFQNGKRV SLSVYLGEFF DIHLFVNGTV TQGDQRVSM PYASKGLYLE TEAGYYKLSG EAYGFVARID GSGNFQVLLS DRYFNKTCGL CGNFNIFAED DFMTQEGTLT S DPYDFANS WALSSGEQWC ERASPPSSSC NISSGEMQKG LWEQCQLLKS TSVFARCHPL VDPEPFVALC EKTLCECAGG LE CACPALL EYARTCAQEG MVLYGWTDHS ACSPVCPAGM EYRQCVSPCA RTCQSLHINE MCQERCVDGC SCPEGQLLDE GLC VESTEC PCVHSGKRYP PGTSLSRDCN TCICRNSQWI CSNEECPGEC LVTGQSHFKS FDNRYFTFSG ICQYLLARDC QDHS FSIVI ETVQCADDRD AVCTRSVTVR LPGLHNSLVK LKHGAGVAMD GQDVQLPLLK GDLRIQHTVT ASVRLSYGED LQMDW DGRG RLLVKLSPVY AGKTCGLCGN YNGNQGDDFL TPSGLAEPRV EDFGNAWKLH GDCQDLQKQH SDPCALNPRM TRFSEE ACA VLTSPTFEAC HRAVSPLPYL RNCRYDVCSC SDGRECLCGA LASYAAACAG RGVRVAWREP GRCELNCPKG QVYLQCG TP CNLTCRSLSY PDEECNEACL EGCFCPPGLY MDERGDCVPK AQCPCYYDGE IFQPEDIFSD HHTMCYCEDG FMHCTMSG V PGSLLPDAVL SSPLSHRSKR UniProtKB: von Willebrand factor |
-Macromolecule #2: von Willebrand factor
Macromolecule | Name: von Willebrand factor / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 54.232809 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: SLSCRPPMVK LVCPADNLRA EGLECTKTCQ NYDLECMSMG CVSGCLCPPG MVRHENRCVA LERCPCFHQG KEYAPGETVK IGCNTCVCQ DRKWNCTDHV CDATCSTIGM AHYLTFDGLK YLFPGECQYV LVQDYCGSNP GTFRILVGNK GCSHPSVKCK K RVTILVEG ...String: SLSCRPPMVK LVCPADNLRA EGLECTKTCQ NYDLECMSMG CVSGCLCPPG MVRHENRCVA LERCPCFHQG KEYAPGETVK IGCNTCVCQ DRKWNCTDHV CDATCSTIGM AHYLTFDGLK YLFPGECQYV LVQDYCGSNP GTFRILVGNK GCSHPSVKCK K RVTILVEG GEIELFDGEV NVKRPMKDET HFEVVESGRY IILLLGKALS VVWDRHLSIS VVLKQTYQEK VCGLCGNFDG IQ NNDLTSS NLQVEEDPVD FGNSWKVSSQ CADTRKVPLD SSPATCHNNI MKQTMVDSSC RILTSDVFQD CNKLVDPEPY LDV CIYDTC SCESIGDCAC FCDTIAAYAH VCAQHGKVVT WRTATLCPQS CEERNLRENG YECEWRYNSC APACQVTCQH PEPL ACPVQ CVEGCHAHCP PGKILDELLQ TCVDPEDCPV CEVAGRRFAS GKKVTLNPSD PEHCQICHCD VVNLTCEACQ EPGGL VVPP HHHHHH UniProtKB: von Willebrand factor |
-Macromolecule #3: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 6 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 8 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ChemComp-NAG: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 154669 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |