1WQ8

Crystal structure of Vammin, a VEGF-F from a snake venom

1WQ8 の概要

• エントリーDOI: 10.2210/pdb1wq8/pdb
• 関連するPDBエントリー: 1WQ9
• 分子名称: Vascular endothelial growth factor toxin, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• 機能のキーワード: snake venom, vascular endothelial growth factor, vegf, vegf-f, toxin
• 由来する生物種: Vipera aspis aspis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12697.64

構造登録者

Suto, K.,Yamazaki, Y.,Morita, T.,Mizuno, H. (登録日: 2004-09-23, 公開日: 2004-12-07, 最終更新日: 2024-10-23)

主引用文献

Suto, K.,Yamazaki, Y.,Morita, T.,Mizuno, H.
Crystal structures of novel vascular endothelial growth factors (VEGF) from snake venoms: insight into selective VEGF binding to kinase insert domain-containing receptor but not to fms-like tyrosine kinase-1.
J.Biol.Chem., 280:2126-2131, 2005

PubMed Abstract: Vascular endothelial growth factor-A (VEGF-A(165)) exerts multiple effects upon binding to the fms-like tyrosine kinase-1 (Flt-1) and the kinase insert domain-containing receptor (KDR). We recently identified two novel snake venom VEGFs (vammin and VR-1) having unique properties. These VEGFs, designated VEGF-Fs, are highly specific ligands for the kinase insert domain-containing receptor and exhibit potent biological activity both in vitro and in vivo when compared with VEGF-A(165). Here, we solved the crystal structures of vammin and VR-1 at 1.9 and 2.0 A resolutions, respectively. Both structures are very similar to each other, and these structures exhibit similar but significantly different features from the known structures of other VEGFs. These differences include a conformational difference in receptor-binding loop 3 caused by an amino acid residue insertion and a difference in surface potential on the possible binding surface for domain 3 of the receptor. These structural differences may be related to the highly selective ligand properties of VEGF-F.

PubMed: 15542594
DOI: 10.1074/jbc.M411395200

実験手法

X-RAY DIFFRACTION (1.9 Å)