1qmr

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[[Image:1qmr.gif|left|200px]]<br /><applet load="1qmr" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qmr.gif|left|200px]]
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caption="1qmr, resolution 2.15&Aring;" />
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'''BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G'''<br />
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{{Structure
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|PDB= 1qmr |SIZE=350|CAPTION= <scene name='initialview01'>1qmr</scene>, resolution 2.15&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= BET V 1 1.2801 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3505 Betula pendula])
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}}
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'''BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QMR 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=1QMR OCA].
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1QMR is a [[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=1QMR OCA].
==Reference==
==Reference==
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Allergy vaccine engineering: epitope modulation of recombinant Bet v 1 reduces IgE binding but retains protein folding pattern for induction of protective blocking-antibody responses., Holm J, Gajhede M, Ferreras M, Henriksen A, Ipsen H, Larsen JN, Lund L, Jacobi H, Millner A, Wurtzen PA, Spangfort MD, J Immunol. 2004 Oct 15;173(8):5258-67. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15470071 15470071]
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Allergy vaccine engineering: epitope modulation of recombinant Bet v 1 reduces IgE binding but retains protein folding pattern for induction of protective blocking-antibody responses., Holm J, Gajhede M, Ferreras M, Henriksen A, Ipsen H, Larsen JN, Lund L, Jacobi H, Millner A, Wurtzen PA, Spangfort MD, J Immunol. 2004 Oct 15;173(8):5258-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15470071 15470071]
[[Category: Betula pendula]]
[[Category: Betula pendula]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: pathogenesis-related protein]]
[[Category: pathogenesis-related protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:48 2008''

Revision as of 11:39, 20 March 2008


PDB ID 1qmr

Drag the structure with the mouse to rotate
, resolution 2.15Å
Gene: BET V 1 1.2801 (Betula pendula)
Coordinates: save as pdb, mmCIF, xml



BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G


Overview

Human type 1 immediate allergic response symptoms are caused by mediator release from basophils and mast cells. This event is triggered by allergens aggregating preformed IgE Abs bound to the high-affinity receptor (FcepsilonRI) on these cells. Thus, the allergen/IgE interaction is crucial for the cascade leading to the allergic and anaphylactic response. Two genetically engineered forms of the white birch pollen major allergen Bet v 1 with point mutations directed at molecular surfaces have been characterized. Four and nine point mutations led to a significant reduction of the binding to human serum IgE, suggesting a mutation-induced distortion of IgE-binding B cell epitopes. In addition, the mutated allergens showed a decrease in anaphylactic potential, because histamine release from human basophils was significantly reduced. Retained alpha-carbon backbone folding pattern of the mutated allergens was indicated by x-ray diffraction analysis and circular dichroism spectroscopy. The rBet v 1 mutants were able to induce proliferation of T cell lines derived from birch pollen allergic patients. The stimulation indices were similar to the indices of nonmutated rBet v 1 and natural Bet v 1 purified from birch pollen. The ability of anti-rBet v 1 mutant specific mouse IgG serum to block binding of human serum IgE to rBet v 1 demonstrates that the engineered rBet v 1 mutants are able to induce Abs reactive with nonmodified Bet v 1. rBet v 1 mutants may constitute vaccine candidates with improved efficacy/safety profiles for safer allergy vaccination.

About this Structure

1QMR is a Single protein structure of sequence from Betula pendula. Full crystallographic information is available from OCA.

Reference

Allergy vaccine engineering: epitope modulation of recombinant Bet v 1 reduces IgE binding but retains protein folding pattern for induction of protective blocking-antibody responses., Holm J, Gajhede M, Ferreras M, Henriksen A, Ipsen H, Larsen JN, Lund L, Jacobi H, Millner A, Wurtzen PA, Spangfort MD, J Immunol. 2004 Oct 15;173(8):5258-67. PMID:15470071

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