1qft | pdb_00001qft

HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS

spinqualitylabelsall models 1qft, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qft is a 2 chain structure with sequence from Rhipicephalus appendiculatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.25Å Ligands: HSM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HBP2_RHIAP Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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