Crystal structure of bitiscetin, a von Willebrand factor-dependent platelet aggregation inducer

S. Hirotsu, H. Mizuno, K. Fukuda, Ma Chun Qi, T. Matsui, J. Hamako, T. Morita, K. Titani

研究成果: Article査読

49 被引用数 (Scopus)

抄録

Bitiscetin, a C-type lectin-like protein isolated from the venom of the snake Bitis arientans, promotes the interactions between plasma von Willebrand factor (VWF) and platelet membrane glycoprotein Ib (GPIb) to induce platelet aggregation. We report here the crystal structure of bitiscetin at 2.0 Å resolution. The overall fold is similar to those of coagulation factor IX/X-binding protein (IX/X-bp) and flavocetin-A (a GPIb-binding protein), although these three proteins are functionally distinct from one another. The characteristic property determining target recognition is explained mainly by the differences in the surface potential on the central concave surface. A negatively charged patch on the surface of bitiscetin is a candidate for the site of binding to the positively charged surface of the VWF A1 domain, as shown in the case of another platelet aggregation inducer, botrocetin. However, a positively charged patch near the central concave surface is unique for bitiscetin and suggests that it is the binding site for the negatively charged surface of the VWF A3 domain. Thus, the interactions accounting for VWF activation by bitiscetin possibly involve both the A1 and A3 domains of VWF, indicating a specific mechanism of VWF activation by bitiscetin.

本文言語English
ページ(範囲)13592-13597
ページ数6
ジャーナルBiochemistry
40
45
DOI
出版ステータスPublished - 13-11-2001

All Science Journal Classification (ASJC) codes

  • 生化学

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