1FVU

CRYSTAL STRUCTURE OF BOTROCETIN

Summary for 1FVU

• Entry DOI: 10.2210/pdb1fvu/pdb
• Descriptor: BOTROCETIN ALPHA CHAIN, BOTROCETIN BETA CHAIN, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: von willbrand factor modulator, c-type lectin, metal-binding, loop exchanged dimer, toxin
• Biological source: Bothrops jararaca (jararaca); More
• Total number of polymer chains: 4
• Total formula weight: 60616.37

Authors

Sen, U.,Vasudevan, S.,Subbarao, G.,McClintoc, R.A.,Celikel, R.,Ruggeri, Z.M.,Varughese, K.I. (deposition date: 2000-09-20, release date: 2001-02-14, Last modification date: 2024-11-20)

Primary citation

Sen, U.,Vasudevan, S.,Subbarao, G.,McClintock, R.A.,Celikel, R.,Ruggeri, Z.M.,Varughese, K.I.
Crystal structure of the von Willebrand factor modulator botrocetin.
Biochemistry, 40:345-352, 2001

PubMed Abstract: 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.

PubMed: 11148028
DOI: 10.1021/bi0021737

Experimental method

X-RAY DIFFRACTION (1.8 Å)