1ktj

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(New page: 200px<br /><applet load="1ktj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ktj, resolution 2.15&Aring;" /> '''X-ray Structure Of D...)
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[[Image:1ktj.gif|left|200px]]<br /><applet load="1ktj" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ktj.gif|left|200px]]<br /><applet load="1ktj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ktj, resolution 2.15&Aring;" />
caption="1ktj, resolution 2.15&Aring;" />
'''X-ray Structure Of Der P 2, The Major House Dust Mite Allergen'''<br />
'''X-ray Structure Of Der P 2, The Major House Dust Mite Allergen'''<br />
==Overview==
==Overview==
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The crystal structure of the common house mite (Dermatophagoides sp.) Der, p 2 allergen was solved at 2.15 A resolution using the MAD phasing, technique, and refined to an R-factor of 0.209. The refined atomic model, which reveals an immunoglobulin-like tertiary fold, differs in important, ways from the previously described NMR structure, because the two, beta-sheets are significantly further apart and create an internal cavity, which is occupied by a hydrophobic ligand. This interaction is, structurally reminiscent of the binding of a prenyl group by a regulatory, protein, the Rho guanine nucleotide exchange inhibitor. The crystal, structure suggests that binding of non-polar molecules may be essential to, the physiological function of the Der p 2 protein.
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The crystal structure of the common house mite (Dermatophagoides sp.) Der p 2 allergen was solved at 2.15 A resolution using the MAD phasing technique, and refined to an R-factor of 0.209. The refined atomic model, which reveals an immunoglobulin-like tertiary fold, differs in important ways from the previously described NMR structure, because the two beta-sheets are significantly further apart and create an internal cavity, which is occupied by a hydrophobic ligand. This interaction is structurally reminiscent of the binding of a prenyl group by a regulatory protein, the Rho guanine nucleotide exchange inhibitor. The crystal structure suggests that binding of non-polar molecules may be essential to the physiological function of the Der p 2 protein.
==About this Structure==
==About this Structure==
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1KTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KTJ OCA].
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1KTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTJ OCA].
==Reference==
==Reference==
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[[Category: Dermatophagoides pteronyssinus]]
[[Category: Dermatophagoides pteronyssinus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Benjamin, D.C.]]
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[[Category: Benjamin, D C.]]
[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
[[Category: Derewenda, U.]]
[[Category: Derewenda, U.]]
[[Category: Derewenda, Z.]]
[[Category: Derewenda, Z.]]
[[Category: Li, J.]]
[[Category: Li, J.]]
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[[Category: Mueller, G.A.]]
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[[Category: Mueller, G A.]]
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[[Category: Rule, G.S.]]
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[[Category: Rule, G S.]]
[[Category: allergen]]
[[Category: allergen]]
[[Category: asthma]]
[[Category: asthma]]
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[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:51:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:47 2008''

Revision as of 11:37, 21 February 2008


1ktj, resolution 2.15Å

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X-ray Structure Of Der P 2, The Major House Dust Mite Allergen

Overview

The crystal structure of the common house mite (Dermatophagoides sp.) Der p 2 allergen was solved at 2.15 A resolution using the MAD phasing technique, and refined to an R-factor of 0.209. The refined atomic model, which reveals an immunoglobulin-like tertiary fold, differs in important ways from the previously described NMR structure, because the two beta-sheets are significantly further apart and create an internal cavity, which is occupied by a hydrophobic ligand. This interaction is structurally reminiscent of the binding of a prenyl group by a regulatory protein, the Rho guanine nucleotide exchange inhibitor. The crystal structure suggests that binding of non-polar molecules may be essential to the physiological function of the Der p 2 protein.

About this Structure

1KTJ is a Single protein structure of sequence from Dermatophagoides pteronyssinus. Full crystallographic information is available from OCA.

Reference

The crystal structure of a major dust mite allergen Der p 2, and its biological implications., Derewenda U, Li J, Derewenda Z, Dauter Z, Mueller GA, Rule GS, Benjamin DC, J Mol Biol. 2002 Apr 19;318(1):189-97. PMID:12054778

Page seeded by OCA on Thu Feb 21 13:37:47 2008

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