1wq8

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

spinqualitylabelsall models 1wq8, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1wq8 is a 1 chain structure with sequence from Vipera aspis aspis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: PCA, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TXVE_VIPAA Snake venom VEGFs may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. The hypotension is mediated by nitric oxide (NO), which is produced by VEGF-activated endothelium NO synthase (PubMed:14600159). Also induces angiogenesis in vitro, probably through VEGF receptor (KDR/VEGFR-2) signaling (PubMed:14600159). May also induce capillary permeability through VEGF receptor (KDR/VEGFR-2) signaling. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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.,Suto K, Yamazaki Y, Morita T, Mizuno H J Biol Chem. 2005 Jan 21;280(3):2126-31. Epub 2004 Nov 12. PMID:15542594 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also VEGF 3D Structures

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