1l3p

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{{STRUCTURE_1l3p| PDB=1l3p | SCENE= }}
{{STRUCTURE_1l3p| PDB=1l3p | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b'''
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===CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b===
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==Overview==
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The major allergen Phlp 5b from timothy grass pollen induces allergic rhinitis and bronchial asthma in millions of allergic patients worldwide. As an important step towards understanding the interactions between the pollen protein and components of the human immune system, the structure of the C-terminal key domain of Phlp 5b has been determined at 2.0 A resolution and refined to an R value of 19.7%. This is the first known allergen composed entirely of alpha-helices. The protein forms a dimer stabilized by one intermolecular disulfide bridge. Sequence homology suggests that at least all group V and group VI grass-pollen allergens belong to this new class of 'four-helix-bundle allergens'.
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(as it appears on PubMed at http://www.pubmed.gov), where 12077438 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12077438}}
==About this Structure==
==About this Structure==
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[[Category: Phl p 5b]]
[[Category: Phl p 5b]]
[[Category: Structure]]
[[Category: Structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:38:21 2008''

Revision as of 08:38, 2 July 2008

Image:1l3p.png

Template:STRUCTURE 1l3p

CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b

Template:ABSTRACT PUBMED 12077438

About this Structure

1L3P is a Single protein structure of sequence from Phleum pratense. Full crystallographic information is available from OCA.

Reference

Structure of the functional domain of the major grass-pollen allergen Phlp 5b., Rajashankar K, Bufe A, Weber W, Eschenburg S, Lindner B, Betzel C, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1175-81. Epub 2002, Jun 20. PMID:12077438

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