1qft

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(New page: 200px<br /><applet load="1qft" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qft, resolution 1.25&Aring;" /> '''HISTAMINE BINDING PR...)
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[[Image:1qft.gif|left|200px]]<br /><applet load="1qft" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qft, resolution 1.25&Aring;" />
caption="1qft, resolution 1.25&Aring;" />
'''HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS'''<br />
'''HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS'''<br />
==Overview==
==Overview==
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High-affinity histamine-binding proteins (HBPs) were discovered in the, saliva of Rhipicephalus appendiculatus ticks. Their ability to outcompete, histamine receptors indicates that they suppress inflammation during blood, feeding. The crystal structure of a histamine-bound HBP, determined at, 1.25 A resolution, reveals a lipocalin fold novel in containing two, binding sites for the same ligand. The sites are orthogonally arranged and, highly rigid and form an internal surface of unusual polar character that, complements the physicochemical properties of histamine. As soluble, receptors of histamine, HBPs offer a new strategy for controlling, histamine-based diseases.
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High-affinity histamine-binding proteins (HBPs) were discovered in the saliva of Rhipicephalus appendiculatus ticks. Their ability to outcompete histamine receptors indicates that they suppress inflammation during blood feeding. The crystal structure of a histamine-bound HBP, determined at 1.25 A resolution, reveals a lipocalin fold novel in containing two binding sites for the same ligand. The sites are orthogonally arranged and highly rigid and form an internal surface of unusual polar character that complements the physicochemical properties of histamine. As soluble receptors of histamine, HBPs offer a new strategy for controlling histamine-based diseases.
==About this Structure==
==About this Structure==
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1QFT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhipicephalus_appendiculatus Rhipicephalus appendiculatus] with HSM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFT OCA].
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1QFT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhipicephalus_appendiculatus Rhipicephalus appendiculatus] with <scene name='pdbligand=HSM:'>HSM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFT OCA].
==Reference==
==Reference==
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[[Category: Rhipicephalus appendiculatus]]
[[Category: Rhipicephalus appendiculatus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Adams, P.L.]]
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[[Category: Adams, P L.]]
[[Category: Harlos, K.]]
[[Category: Harlos, K.]]
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[[Category: Nuttal, P.A.]]
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[[Category: Nuttal, P A.]]
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[[Category: Paesen, G.C.]]
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[[Category: Paesen, G C.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
[[Category: HSM]]
[[Category: HSM]]
[[Category: lipocalin]]
[[Category: lipocalin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:39:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:01 2008''

Revision as of 12:39, 21 February 2008


1qft, resolution 1.25Å

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HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS

Overview

High-affinity histamine-binding proteins (HBPs) were discovered in the saliva of Rhipicephalus appendiculatus ticks. Their ability to outcompete histamine receptors indicates that they suppress inflammation during blood feeding. The crystal structure of a histamine-bound HBP, determined at 1.25 A resolution, reveals a lipocalin fold novel in containing two binding sites for the same ligand. The sites are orthogonally arranged and highly rigid and form an internal surface of unusual polar character that complements the physicochemical properties of histamine. As soluble receptors of histamine, HBPs offer a new strategy for controlling histamine-based diseases.

About this Structure

1QFT is a Single protein structure of sequence from Rhipicephalus appendiculatus with as ligand. Full crystallographic information is available from OCA.

Reference

Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure., Paesen GC, Adams PL, Harlos K, Nuttall PA, Stuart DI, Mol Cell. 1999 May;3(5):661-71. PMID:10360182

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