1qnx
From Proteopedia
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- | [[Image:1qnx.jpg|left|200px]] | + | [[Image:1qnx.jpg|left|200px]] |
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- | '''VES V 5, AN ALLERGEN FROM VESPULA VULGARIS VENOM''' | + | {{Structure |
+ | |PDB= 1qnx |SIZE=350|CAPTION= <scene name='initialview01'>1qnx</scene>, resolution 1.90Å | ||
+ | |SITE= <scene name='pdbsite=NA1:Na+Binding+Site+For+Residue+A458'>NA1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''VES V 5, AN ALLERGEN FROM VESPULA VULGARIS VENOM''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1QNX is a [ | + | 1QNX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vespula_vulgaris Vespula vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNX OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11746691 11746691] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vespula vulgaris]] | [[Category: Vespula vulgaris]] | ||
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[[Category: vespid venom]] | [[Category: vespid venom]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:16 2008'' |
Revision as of 11:40, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
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. 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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