1QFT

HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.25 Å
  • R-Value Work: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure.

Paesen, G.C., Adams, P.L., Harlos, K., Nuttall, P.A., Stuart, D.I.

(1999) Mol Cell 3: 661-671

  • DOI: https://doi.org/10.1016/s1097-2765(00)80359-7
  • Primary Citation of Related Structures:  
    1QFT, 1QFV

  • 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.

    • Organizational Affiliation: 

    Natural Environment Research Council, Institute of Virology and Environmental Microbiology, Oxford, United Kingdom. gcp@mail.nerc-oxford.ac.uk


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (FEMALE-SPECIFIC HISTAMINE BINDING PROTEIN 2)
A, B
175Rhipicephalus appendiculatusMutation(s): 0 
UniProt
Find proteins for O77421 (Rhipicephalus appendiculatus)
Explore O77421 
Go to UniProtKB:  O77421
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO77421
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
HSM PDBBind:  1QFT Kd: 1.7 (nM) from 1 assay(s)
Binding MOAD:  1QFT Kd: 1.7 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.25 Å
  • R-Value Work: 0.184 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.42α = 90
b = 74.79β = 90
c = 78.52γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
X-PLORrefinement

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-04-19
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations