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1xwv
From Proteopedia
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|PDB= 1xwv |SIZE=350|CAPTION= <scene name='initialview01'>1xwv</scene>, resolution 1.83Å | |PDB= 1xwv |SIZE=350|CAPTION= <scene name='initialview01'>1xwv</scene>, resolution 1.83Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PE3:3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL'>PE3</scene> | + | |LIGAND= <scene name='pdbligand=PE3:3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL'>PE3</scene>, <scene name='pdbligand=XPE:3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL'>XPE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xwv OCA], [http://www.ebi.ac.uk/pdbsum/1xwv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xwv RCSB]</span> | ||
}} | }} | ||
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[[Category: Skov, L K.]] | [[Category: Skov, L K.]] | ||
[[Category: Spangfort, M.]] | [[Category: Spangfort, M.]] | ||
| - | [[Category: PE3]] | ||
| - | [[Category: XPE]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:55:47 2008'' |
Revision as of 21:55, 30 March 2008
| |||||||
| , resolution 1.83Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the house dust mite allergen Der f 2: Implications for function and molecular basis of IgE cross-reactivity
Overview
The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.
About this Structure
1XWV is a Single protein structure of sequence from Dermatophagoides farinae. Full crystallographic information is available from OCA.
Reference
Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity., Johannessen BR, Skov LK, Kastrup JS, Kristensen O, Bolwig C, Larsen JN, Spangfort M, Lund K, Gajhede M, FEBS Lett. 2005 Feb 14;579(5):1208-12. Epub 2005 Jan 21. PMID:15710415
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