1fvu
From Proteopedia
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CRYSTAL STRUCTURE OF BOTROCETIN
Overview
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.
About this Structure
1FVU is a Protein complex structure of sequences from Bothrops jararaca with MG as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the von Willebrand factor modulator botrocetin., Sen U, Vasudevan S, Subbarao G, McClintock RA, Celikel R, Ruggeri ZM, Varughese KI, Biochemistry. 2001 Jan 16;40(2):345-52. PMID:11148028
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