1fvu

CRYSTAL STRUCTURE OF BOTROCETIN

spinqualitylabelsall models 1fvu, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fvu is a 4 chain structure with sequence from Bothrops jararaca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LECBA_BOTJA] Snaclec that activates platelets by targeting vWF/GPIb. Two-chain botrocetin forms an activated complex with vWF (by binding the A1 domain), and the complex then binds to platelet glycoprotein Ibalpha (GP1BA), resulting in platelet aggregation. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets. [LECBB_BOTJA] Snaclec that activates platelets by targeting vWF/GPIb. Two-chain botrocetin forms an activated complex with vWF (by binding the A1 domain), and the complex then binds to platelet glycoprotein Ibalpha (GP1BA), resulting in platelet aggregation. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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