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Structure paper

TitleTowards the Structural Basis of Regulation of Von Willebrand Factor Binding to Glycoprotein Ib
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 5565-, Year 2014
Publish dateAug 16, 2013 (structure data deposition date)
AuthorsBlenner, M.A. / Dong, X. / Springer, T.A.
External linksJ. Biol. Chem. / PubMed:24391089
MethodsX-ray diffraction
Resolution2.081 - 2.8 Å
Structure data

PDB-4c29:
Crystal Structure of High-Affinity von Willebrand Factor A1 domain with Disulfide Mutation
Method: X-RAY DIFFRACTION / Resolution: 2.202 Å

PDB-4c2a:
Crystal Structure of High-Affinity von Willebrand Factor A1 domain with R1306Q and I1309V Mutations in Complex with High Affinity GPIb alpha
Method: X-RAY DIFFRACTION / Resolution: 2.081 Å

PDB-4c2b:
Crystal Structure of High-Affinity von Willebrand Factor A1 domain with Disulfide Mutation in Complex with High Affinity GPIb alpha
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CAC:
CACODYLATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • homo sapiens (human)
KeywordsBLOOD CLOTTING / CELL ADHESION / A1 / GPIBALPHA

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