1btv
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btv OCA], [http://www.ebi.ac.uk/pdbsum/1btv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1btv RCSB]</span> | ||
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[[Category: pr-10 protein]] | [[Category: pr-10 protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:12 2008'' |
Revision as of 16:08, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF BET V 1, NMR, 20 STRUCTURES
Overview
The three-dimensional structure of the major birch pollen allergen, the 17,500 M(r) acidic protein Bet v 1 (from the birch, Betula verrucosa), is presented as determined both in the crystalline state by X-ray diffraction and in solution by nuclear magnetic resonance (NMR) spectroscopy. This is the first experimentally determined structure of a clinically important inhalant major allergen, estimated to cause allergy in 5-10 million individuals worldwide. The structure shows three regions on the molecular surface predicted to harbour cross-reactive B-cell epitopes which provide a structural basis for the allergic symptoms that birch pollen allergic patients show when they encounter pollens from related trees such as hazel, alder and hornbeam. The structure also shows an unusual feature, a 30 A-long forked cavity that penetrates the entire protein.
About this Structure
1BTV is a Single protein structure of sequence from Betula pendula. Full crystallographic information is available from OCA.
Reference
X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy., Gajhede M, Osmark P, Poulsen FM, Ipsen H, Larsen JN, Joost van Neerven RJ, Schou C, Lowenstein H, Spangfort MD, Nat Struct Biol. 1996 Dec;3(12):1040-5. PMID:8946858
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