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Tick histamine-binding proteins: lipocalins with a second binding cavity.

G C Paesen1, P L Adams, P A Nuttall

  • 1CEH Institute of Virology and Environmental Microbiology, Oxford, UK. gcp@ceh.ac.uk

Biochimica Et Biophysica Acta
|November 4, 2000
PubMed
Summary

Tick histamine-binding proteins (HBPs) are unique lipocalins with two distinct histamine binding sites. These proteins have evolved specialized structures to bind hydrophilic molecules, unlike other lipocalins.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Tick histamine-binding proteins (HBPs) are a subclass of lipocalins.
  • Lipocalins typically bind hydrophobic molecules within a beta-barrel structure.
  • HBPs possess unique structural adaptations for binding histamine.

Purpose of the Study:

  • To investigate the structural characteristics of tick histamine-binding proteins.
  • To understand the molecular basis for histamine binding in HBPs.
  • To compare the structure of HBPs to other lipocalins.

Main Methods:

  • Structural analysis of tick histamine-binding proteins.
  • Comparison of HBP structures with known lipocalin structures.
  • Analysis of amino acid composition within binding pockets.

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Main Results:

  • HBPs possess two distinct histamine binding pockets.
  • A second, low-affinity binding site is located at the 'closed-end' of the beta-barrel, a region typically inaccessible in other lipocalins.
  • The 'closed-end' region in HBPs shows significant structural divergence from other lipocalins, including the loss of a 3(10) helix and conserved residues, and the addition of an alpha-helix shielding the cavity.
  • HBP binding pockets are characterized by a high proportion of acidic residues, facilitating the binding of cationic, hydrophilic molecules like histamine.

Conclusions:

  • Tick histamine-binding proteins exhibit unique structural modifications compared to canonical lipocalins.
  • These adaptations enable HBPs to bind hydrophilic, cationic molecules such as histamine, contrasting with the hydrophobic binding typical of other lipocalins.
  • The specialized structure of HBPs reflects an evolutionary adaptation for interacting with histamine in the tick's biological context.