1qnx
From Proteopedia
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VES V 5, AN ALLERGEN FROM VESPULA VULGARIS VENOM
Overview
Ves v 5 is one of three major allergens found in yellow-jacket venom:, phospholipase A(1) (Ves v 1), hyaluronidase (Ves v 2), and antigen 5 (Ves, v 5). Ves v 5 is related by high amino acid sequence identity to, pathogenesis-related proteins including proteins from mammals, reptiles, insects, fungi, and plants. The crystal structure of Ves v 5 has been, solved and refined to a resolution of 1.9 A. The majority of residues, conserved between the pathogenesis-related proteins can be rationalized in, terms of hydrogen bonding patterns and hydrophobic interactions defining, an alpha-beta-alpha sandwich core structure. A small number of consensus, residues are solvent exposed (including two adjacent histidines) and, located in an elongated cavity that forms a putative active site. The site, has no structural resemblance to previously characterized enzymes., Homologous antigen 5's from a large number of different yellow jackets, hornets, and paper wasps are known and patients show varying extents of, cross-reactivity to the related antigen 5's. The structure of Ves v 5, allows a detailed analysis of the epitopes that may participate in, antigenic cross-reactivity, findings that are useful for the development, of a vaccine for treatment of insect allergy.
About this Structure
1QNX is a Single protein structure of sequence from Vespula vulgaris with NA as ligand. Structure known Active Site: NA1. Full crystallographic information is available from OCA.
Reference
Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily., Henriksen A, King TP, Mirza O, Monsalve RI, Meno K, Ipsen H, Larsen JN, Gajhede M, Spangfort MD, Proteins. 2001 Dec 1;45(4):438-48. PMID:11746691
Page seeded by OCA on Mon Nov 5 17:02:56 2007
