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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[[Image:1btv.gif|left|200px]]<br /><applet load="1btv" size="350" color="white" frame="true" align="right" spinBox="true"
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'''STRUCTURE OF BET V 1, NMR, 20 STRUCTURES'''<br />
'''STRUCTURE OF BET V 1, NMR, 20 STRUCTURES'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1BTV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Betula_pendula Betula pendula]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BTV OCA].
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1BTV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Betula_pendula Betula pendula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTV OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gajhede, M.]]
[[Category: Gajhede, M.]]
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[[Category: Larsen, J.N.]]
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[[Category: Larsen, J N.]]
[[Category: Osmark, P.]]
[[Category: Osmark, P.]]
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[[Category: Poulsen, F.M.]]
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[[Category: Poulsen, F M.]]
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[[Category: Spangfort, M.D.]]
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[[Category: Spangfort, M D.]]
[[Category: ige-allergy]]
[[Category: ige-allergy]]
[[Category: major birch pollen allergen]]
[[Category: major birch pollen allergen]]
[[Category: pr-10 protein]]
[[Category: pr-10 protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:54:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:02 2008''

Revision as of 09:59, 21 February 2008


1btv

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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

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