1qft

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[[Image:1qft.gif|left|200px]]
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{{STRUCTURE_1qft| PDB=1qft | SCENE= }}
{{STRUCTURE_1qft| PDB=1qft | SCENE= }}
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'''HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS'''
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===HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 10360182 is the PubMed ID number.
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==About this Structure==
==About this Structure==
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[[Category: Stuart, D I.]]
[[Category: Stuart, D I.]]
[[Category: Lipocalin]]
[[Category: Lipocalin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:47:59 2008''

Revision as of 04:48, 28 July 2008

Image:1qft.png

Template:STRUCTURE 1qft

HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS

Template:ABSTRACT PUBMED 10360182

About this Structure

1QFT is a Single protein structure of sequence from Rhipicephalus appendiculatus. 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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