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PDBsum entry 1fvu
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the von willebrand factor modulator botrocetin.
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Authors
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U.Sen,
S.Vasudevan,
G.Subbarao,
R.A.Mcclintock,
R.Celikel,
Z.M.Ruggeri,
K.I.Varughese.
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Ref.
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Biochemistry, 2001,
40,
345-352.
[DOI no: ]
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PubMed id
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Abstract
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The binding of von Willebrand factor (vWF) to the platelet receptor,
glycoprotein (GP) Ib-IX-V complex, has a key role in the initiation of thrombus
formation and is regulated by interactions with extracellular matrix components
under the influence of hemodynamic forces. To a certain extent, these effects
can be mimicked in vitro by two nonphysiologic modulators, ristocetin and
botrocetin. The latter, isolated from the venom of the snake Bothrops jararaca,
is a 31-kDa heterodimeric protein that forms a soluble complex with vWF. As an
initial step toward understanding the mechanisms that regulate vWF function, we
have solved the crystal structure of botrocetin at 1.8 A resolution. Botrocetin
exhibits homology with other snake proteins, but contains only one metal binding
site as compared to two in Factor IX binding protein and Factor IX/X binding
protein and none in flavocetin. A distinctive feature of botrocetin is the
presence of a negatively charged surface that may play a role in the association
with the vWF A1 domain.
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