1QFT

HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS

Summary for 1QFT

• Entry DOI: 10.2210/pdb1qft/pdb
• Descriptor: PROTEIN (FEMALE-SPECIFIC HISTAMINE BINDING PROTEIN 2), HISTAMINE (3 entities in total)
• Functional Keywords: lipocalin, ligand binding protein
• Biological source: Rhipicephalus appendiculatus
• Cellular location: Secreted: O77421
• Total number of polymer chains: 2
• Total formula weight: 40065.46

Authors

Paesen, G.C.,Adams, P.L.,Harlos, K.,Nuttal, P.A.,Stuart, D.I. (deposition date: 1999-04-14, release date: 2000-04-19, Last modification date: 2024-10-16)

Primary citation

Paesen, G.C.,Adams, P.L.,Harlos, K.,Nuttall, P.A.,Stuart, D.I.
Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure.
Mol.Cell, 3:661-671, 1999

PubMed Abstract: 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.

PubMed: 10360182
DOI: 10.1016/S1097-2765(00)80359-7

Experimental method

X-RAY DIFFRACTION (1.25 Å)