1pxz

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(New page: 200px<br /><applet load="1pxz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pxz, resolution 1.70&Aring;" /> '''1.7 Angstrom Crystal...)
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[[Image:1pxz.gif|left|200px]]<br /><applet load="1pxz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pxz, resolution 1.70&Aring;" />
caption="1pxz, resolution 1.70&Aring;" />
'''1.7 Angstrom Crystal Structure of jun a 1, the major allergen from cedar pollen'''<br />
'''1.7 Angstrom Crystal Structure of jun a 1, the major allergen from cedar pollen'''<br />
==Overview==
==Overview==
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Pollen from cedar and cypress trees is a major cause of seasonal, hypersensitivity in humans in several regions of the Northern Hemisphere., We report the first crystal structure of a cedar allergen, Jun a 1, from, the pollen of the mountain cedar Juniperus ashei (Cupressaceae). The core, of the structure consists primarily of a parallel beta-helix, which is, nearly identical to that found in the pectin/pectate lyases from several, plant pathogenic microorganisms. Four IgE epitopes mapped to the surface, of the protein are accessible to the solvent. The conserved vWiDH sequence, is covered by the first 30 residues of the N terminus. The potential, reactive arginine, analogous to the pectin/pectate lyase reaction site, is, accessible to the solvent, but the substrate binding groove is blocked by, a histidine-aspartate salt bridge, a glutamine, and an alpha-helix, all of, which are unique to Jun a 1. These observations suggest that steric, hindrance in Jun a 1 precludes enzyme activity. The overall results, suggest that it is the structure of Jun a 1 that makes it a potent, allergen.
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Pollen from cedar and cypress trees is a major cause of seasonal hypersensitivity in humans in several regions of the Northern Hemisphere. We report the first crystal structure of a cedar allergen, Jun a 1, from the pollen of the mountain cedar Juniperus ashei (Cupressaceae). The core of the structure consists primarily of a parallel beta-helix, which is nearly identical to that found in the pectin/pectate lyases from several plant pathogenic microorganisms. Four IgE epitopes mapped to the surface of the protein are accessible to the solvent. The conserved vWiDH sequence is covered by the first 30 residues of the N terminus. The potential reactive arginine, analogous to the pectin/pectate lyase reaction site, is accessible to the solvent, but the substrate binding groove is blocked by a histidine-aspartate salt bridge, a glutamine, and an alpha-helix, all of which are unique to Jun a 1. These observations suggest that steric hindrance in Jun a 1 precludes enzyme activity. The overall results suggest that it is the structure of Jun a 1 that makes it a potent allergen.
==About this Structure==
==About this Structure==
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1PXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Juniperus_ashei Juniperus ashei]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PXZ OCA].
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1PXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Juniperus_ashei Juniperus ashei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXZ OCA].
==Reference==
==Reference==
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[[Category: Juniperus ashei]]
[[Category: Juniperus ashei]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brooks, E.G.]]
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[[Category: Brooks, E G.]]
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[[Category: Czerwinski, E.W.]]
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[[Category: Czerwinski, E W.]]
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[[Category: Goldblum, R.M.]]
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[[Category: Goldblum, R M.]]
[[Category: Midoro-Horiuti, T.]]
[[Category: Midoro-Horiuti, T.]]
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[[Category: White, M.A.]]
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[[Category: White, M A.]]
[[Category: allergen]]
[[Category: allergen]]
[[Category: cedar pollen]]
[[Category: cedar pollen]]
[[Category: parallel beta-helix]]
[[Category: parallel beta-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:13:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:44 2008''

Revision as of 12:33, 21 February 2008


1pxz, resolution 1.70Å

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1.7 Angstrom Crystal Structure of jun a 1, the major allergen from cedar pollen

Overview

Pollen from cedar and cypress trees is a major cause of seasonal hypersensitivity in humans in several regions of the Northern Hemisphere. We report the first crystal structure of a cedar allergen, Jun a 1, from the pollen of the mountain cedar Juniperus ashei (Cupressaceae). The core of the structure consists primarily of a parallel beta-helix, which is nearly identical to that found in the pectin/pectate lyases from several plant pathogenic microorganisms. Four IgE epitopes mapped to the surface of the protein are accessible to the solvent. The conserved vWiDH sequence is covered by the first 30 residues of the N terminus. The potential reactive arginine, analogous to the pectin/pectate lyase reaction site, is accessible to the solvent, but the substrate binding groove is blocked by a histidine-aspartate salt bridge, a glutamine, and an alpha-helix, all of which are unique to Jun a 1. These observations suggest that steric hindrance in Jun a 1 precludes enzyme activity. The overall results suggest that it is the structure of Jun a 1 that makes it a potent allergen.

About this Structure

1PXZ is a Single protein structure of sequence from Juniperus ashei. Full crystallographic information is available from OCA.

Reference

Crystal structure of Jun a 1, the major cedar pollen allergen from Juniperus ashei, reveals a parallel beta-helical core., Czerwinski EW, Midoro-Horiuti T, White MA, Brooks EG, Goldblum RM, J Biol Chem. 2005 Feb 4;280(5):3740-6. Epub 2004 Nov 10. PMID:15539389

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