1QNX

Ves v 5, an allergen from Vespula vulgaris venom

Summary for 1QNX

• Entry DOI: 10.2210/pdb1qnx/pdb
• Descriptor: VES V 5, SODIUM ION (3 entities in total)
• Functional Keywords: antigen 5, allergen, vespid venom
• Biological source: VESPULA VULGARIS (YELLOW JACKET)
• Cellular location: Secreted: Q05110
• Total number of polymer chains: 1
• Total formula weight: 23885.07

Authors

Henriksen, A.,Gajhede, M.,Spangfort, M.D. (deposition date: 1999-10-25, release date: 2000-10-26, Last modification date: 2024-11-20)

Primary citation

Henriksen, A.,King, T.P.,Mirza, O.,Monsalve, R.I.,Meno, K.,Ipsen, H.,Larsen, J.N.,Gajhede, M.,Spangfort, M.D.
Major Venom Allergen of Yellow Jackets, Ves V 5: Structural Characterization of a Pathogenesis-Related Protein Superfamily.
Proteins: Struct.,Funct., Genet., 45:438-, 2001

PubMed Abstract: 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.

PubMed: 11746691
DOI: 10.1002/PROT.1160

Experimental method

X-RAY DIFFRACTION (1.9 Å)