1JWI
Crystal Structure of Bitiscetin, a von Willeband Factor-dependent Platelet Aggregation Inducer.
1JWI の概要
| エントリーDOI | 10.2210/pdb1jwi/pdb |
| 分子名称 | bitiscetin, platelet aggregation inducer (3 entities in total) |
| 機能のキーワード | domain swapping, c-type lectin, toxin |
| 由来する生物種 | Bitis arietans (puff adder) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 29775.82 |
| 構造登録者 | Hirotsu, S.,Mizuno, H.,Fukuda, K.,Qi, M.C.,Matsui, T.,Hamako, J.,Morita, T.,Titani, K. (登録日: 2001-09-04, 公開日: 2001-11-28, 最終更新日: 2024-10-23) |
| 主引用文献 | Hirotsu, S.,Mizuno, H.,Fukuda, K.,Qi, M.C.,Matsui, T.,Hamako, J.,Morita, T.,Titani, K. Crystal structure of bitiscetin, a von Willebrand factor-dependent platelet aggregation inducer. Biochemistry, 40:13592-13597, 2001 Cited by PubMed Abstract: 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 A 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. PubMed: 11695907DOI: 10.1021/bi0114933 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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