1qft
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qft OCA], [http://www.ebi.ac.uk/pdbsum/1qft PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qft RCSB]</span> | ||
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[[Category: Paesen, G C.]] | [[Category: Paesen, G C.]] | ||
[[Category: Stuart, D I.]] | [[Category: Stuart, D I.]] | ||
| - | [[Category: HSM]] | ||
[[Category: lipocalin]] | [[Category: lipocalin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:55 2008'' |
Revision as of 20:12, 30 March 2008
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| , resolution 1.25Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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