3GPR

Crystal structure of rhodocetin

3GPR の概要

• エントリーDOI: 10.2210/pdb3gpr/pdb
• 分子名称: Rhodocetin subunit alpha, Rhodocetin subunit beta, Rhodocetin subunit gamma, ... (4 entities in total)
• 機能のキーワード: rhodocetin, disulfide bond, lectin, secreted, toxin, cell adhesion
• 由来する生物種: Calloselasma rhodostoma (Malayan pit viper); 詳細
• 細胞内の位置: Secreted: P81397 P81398
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61550.55

構造登録者

Stetefeld, J. (登録日: 2009-03-23, 公開日: 2009-12-15, 最終更新日: 2024-11-20)

主引用文献

Eble, J.A.,Niland, S.,Bracht, T.,Mormann, M.,Peter-Katalinic, J.,Pohlentz, G.,Stetefeld, J.
The alpha2beta1 integrin-specific antagonist rhodocetin is a cruciform, heterotetrameric molecule
Faseb J., 23:2917-2927, 2009

PubMed Abstract: The integrin alpha2beta1 plays an important role in various pathophysiological processes, such as thrombosis, wound healing, inflammation, and metastasis. Rhodocetin, a constituent of the venom of the hemorrhagic Malayan pit viper (Calloselasma rhodostoma), is a specific alpha2beta1 integrin antagonist. To understand its molecular mode of action, its structure was studied by crystallography. Its quaternary structure in solution was also analyzed biochemically. Two novel subunits of rhodocetin were sequenced by mass spectrometry. Their integrin binding was measured by protein interaction ELISAs. Rhodocetin is a C-type lectin-like protein (CLP) consisting of four homologous, yet distinct, subunits, alpha, beta, gamma, and delta, the latter two of which have been unknown to date. With their CLP folds and loop-swapping motifs, the subunits alpha, beta and gamma, delta form two heterodimeric pairs. Uniquely, they arrange orthogonally and shape a cruciform molecule. Bearing a single unpaired cysteine residue, rhodocetin can only form covalent supramolecular complexes with a maximum aggregation number of 2, unlike many heterodimeric CLPs. Being the first heterotetrameric CLP to be crystallized, rhodocetin provides not only the prototypic molecular structure for heterotetrameric CLPs, but also a lead structure for pharmaceutical alpha2beta1 integrin antagonists.

PubMed: 19369383
DOI: 10.1096/fj.08-126763

実験手法

X-RAY DIFFRACTION (3.2 Å)