1C3A

CRYSTAL STRUCTURE OF FLAVOCETIN-A FROM THE HABU SNAKE VENOM, A NOVEL CYCLIC TETRAMER OF C-TYPE LECTIN-LIKE HETERODIMERS

1C3A の概要

• エントリーDOI: 10.2210/pdb1c3a/pdb
• 分子名称: FLAVOCETIN-A: ALPHA SUBUNIT, FLAVOCETIN-A: BETA SUBUNIT (3 entities in total)
• 機能のキーワード: c-type lectin-like domains, membrane protein
• 由来する生物種: Trimeresurus flavoviridis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30230.68

構造登録者

Fukuda, K.,Mizuno, H.,Atoda, H.,Morita, T. (登録日: 1999-07-27, 公開日: 2000-03-06, 最終更新日: 2024-10-30)

主引用文献

Fukuda, K.,Mizuno, H.,Atoda, H.,Morita, T.
Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers.
Biochemistry, 39:1915-1923, 2000

PubMed Abstract: Snake venom contains a number of the hemostatically active C-type lectin-like proteins, which affect the interaction between von Willebrand factor (vWF) and the platelet glycoprotein (GP) Ib or platelet receptor to inhibit/induce platelet activation. Flavocetin-A (FL-A) is a high-molecular mass C-type lectin-like protein (149 kDa) isolated from the habu snake venom. FL-A binds with high affinity to the platelet GP Ibalpha-subunit and functions as a strong inhibitor of vWF-dependent platelet aggregation. We have determined the X-ray crystal structure of FL-A and refined to 2.5 A resolution. This is a first elucidation of a three-dimensional structure of the platelet GP Ib-binding protein. The overall structure reveals that the molecule is a novel cyclic tetramer (alphabeta)(4) made up of four alphabeta-heterodimers related by a crystallographic 4-fold symmetry. The tetramerization is mediated by an interchain disulfide bridge between cysteine residues at the C-terminus of the alpha-subunit and at the N-terminus of the beta-subunit in the neighboring alphabeta-heterodimer. The high affinity of FL-A for the platelet GP Ib alpha-subunit could be explained by a cooperative-binding action through the multiple binding sites of the tetramer.

PubMed: 10684640
DOI: 10.1021/bi992134z

実験手法

X-RAY DIFFRACTION (2.5 Å)