1qnx
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Ves v 5 is one of three major allergens found in yellow-jacket venom: | + | 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== | ==About this Structure== | ||
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[[Category: Gajhede, M.]] | [[Category: Gajhede, M.]] | ||
[[Category: Henriksen, A.]] | [[Category: Henriksen, A.]] | ||
| - | [[Category: Spangfort, M | + | [[Category: Spangfort, M D.]] |
[[Category: NA]] | [[Category: NA]] | ||
[[Category: allergen]] | [[Category: allergen]] | ||
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[[Category: vespid venom]] | [[Category: vespid venom]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:48 2008'' |
Revision as of 12:41, 21 February 2008
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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 as ligand. Known structural/functional Site: . 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
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