2jmh

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==Overview==
==Overview==
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Blo t 5 is the major allergen from Blomia tropicalis mites and shows, strong IgE reactivity with up to 90% of asthmatic and rhinitis patients', sera. The NMR solution structure of Blo t 5 comprises three long alpha, helices, forming a coiled-coil, triple-helical bundle with a left-handed, twist. TROSY-NMR experiments were used to study Blo t 5 interaction with, the Fab' of a specific monoclonal antibody, mAb 4A7. The mAb epitope, comprises two closely spaced surfaces, I and II, connected by a sharp turn, and bearing critical residues Asn46 and Lys47 on one surface, and Lys54, and Arg57 on the other. This discontinuous epitope overlaps with the human, IgE epitope(s) of Blo t 5. Epitope surface II is further predicted to, undergo conformational exchange in the millisecond to microsecond range., The results presented are critical for the design of a hypoallergenic Blo, t 5 for efficacious immunotherapy of allergic diseases.
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Blo t 5 is the major allergen from Blomia tropicalis mites and shows strong IgE reactivity with up to 90% of asthmatic and rhinitis patients' sera. The NMR solution structure of Blo t 5 comprises three long alpha helices, forming a coiled-coil, triple-helical bundle with a left-handed twist. TROSY-NMR experiments were used to study Blo t 5 interaction with the Fab' of a specific monoclonal antibody, mAb 4A7. The mAb epitope comprises two closely spaced surfaces, I and II, connected by a sharp turn and bearing critical residues Asn46 and Lys47 on one surface, and Lys54 and Arg57 on the other. This discontinuous epitope overlaps with the human IgE epitope(s) of Blo t 5. Epitope surface II is further predicted to undergo conformational exchange in the millisecond to microsecond range. The results presented are critical for the design of a hypoallergenic Blo t 5 for efficacious immunotherapy of allergic diseases.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Roles of Structure and Structural Dynamics in the Antibody Recognition of the Allergen Proteins: An NMR Study on Blomia tropicalis Major Allergen., Naik MT, Chang CF, Kuo IC, Kung CC, Yi FC, Chua KY, Huang TH, Structure. 2008 Jan;16(1):125-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18184590 18184590]
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Roles of structure and structural dynamics in the antibody recognition of the allergen proteins: an NMR study on Blomia tropicalis major allergen., Naik MT, Chang CF, Kuo IC, Kung CC, Yi FC, Chua KY, Huang TH, Structure. 2008 Jan;16(1):125-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18184590 18184590]
[[Category: Blomia tropicalis]]
[[Category: Blomia tropicalis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Huang, T.]]
[[Category: Huang, T.]]
[[Category: Kuo, I.]]
[[Category: Kuo, I.]]
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[[Category: Naik, M.T.]]
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[[Category: Naik, M T.]]
[[Category: allergen]]
[[Category: allergen]]
[[Category: blo t 5]]
[[Category: blo t 5]]
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[[Category: group 5]]
[[Category: group 5]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:39:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:03 2008''

Revision as of 16:04, 21 February 2008


2jmh

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NMR solution structure of Blo t 5, a major mite allergen from Blomia tropicalis

Overview

Blo t 5 is the major allergen from Blomia tropicalis mites and shows strong IgE reactivity with up to 90% of asthmatic and rhinitis patients' sera. The NMR solution structure of Blo t 5 comprises three long alpha helices, forming a coiled-coil, triple-helical bundle with a left-handed twist. TROSY-NMR experiments were used to study Blo t 5 interaction with the Fab' of a specific monoclonal antibody, mAb 4A7. The mAb epitope comprises two closely spaced surfaces, I and II, connected by a sharp turn and bearing critical residues Asn46 and Lys47 on one surface, and Lys54 and Arg57 on the other. This discontinuous epitope overlaps with the human IgE epitope(s) of Blo t 5. Epitope surface II is further predicted to undergo conformational exchange in the millisecond to microsecond range. The results presented are critical for the design of a hypoallergenic Blo t 5 for efficacious immunotherapy of allergic diseases.

About this Structure

2JMH is a Single protein structure of sequence from Blomia tropicalis. Full crystallographic information is available from OCA.

Reference

Roles of structure and structural dynamics in the antibody recognition of the allergen proteins: an NMR study on Blomia tropicalis major allergen., Naik MT, Chang CF, Kuo IC, Kung CC, Yi FC, Chua KY, Huang TH, Structure. 2008 Jan;16(1):125-36. PMID:18184590

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