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1btv
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(New page: 200px<br /><applet load="1btv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1btv" /> '''STRUCTURE OF BET V 1, NMR, 20 STRUCTURES'''<...)
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Revision as of 09:47, 20 November 2007
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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
Page seeded by OCA on Tue Nov 20 11:54:57 2007
