1l3p

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(New page: 200px<br /><applet load="1l3p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3p, resolution 1.98&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1l3p.jpg|left|200px]]<br /><applet load="1l3p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1l3p, resolution 1.98&Aring;" />
caption="1l3p, resolution 1.98&Aring;" />
'''CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b'''<br />
'''CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b'''<br />
==Overview==
==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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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'.
==About this Structure==
==About this Structure==
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1L3P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phleum_pratense Phleum pratense] with PO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L3P OCA].
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1L3P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phleum_pratense Phleum pratense] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3P OCA].
==Reference==
==Reference==
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[[Category: Eschenburg, S.]]
[[Category: Eschenburg, S.]]
[[Category: Lindner, B.]]
[[Category: Lindner, B.]]
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[[Category: Rajashankar, K.R.]]
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[[Category: Rajashankar, K R.]]
[[Category: Weber, W.]]
[[Category: Weber, W.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: structure]]
[[Category: structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:13:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:58 2008''

Revision as of 11:41, 21 February 2008


1l3p, resolution 1.98Å

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

Overview

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'.

About this Structure

1L3P is a Single protein structure of sequence from Phleum pratense with and as ligands. 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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