1qft
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HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS
OverviewOverview
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 StructureAbout this Structure
1QFT is a Single protein structure of sequence from Rhipicephalus appendiculatus with HSM as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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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