Format

Send to

Choose Destination
See comment in PubMed Commons below
J Mol Biol. 2002 Apr 19;318(1):189-97.

The crystal structure of a major dust mite allergen Der p 2, and its biological implications.

Author information

  • 1Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA. ud3a@virginia.edu

Abstract

The crystal structure of the common house mite (Dermatophagoides sp.) Der p 2 allergen was solved at 2.15 A resolution using the MAD phasing technique, and refined to an R-factor of 0.209. The refined atomic model, which reveals an immunoglobulin-like tertiary fold, differs in important ways from the previously described NMR structure, because the two beta-sheets are significantly further apart and create an internal cavity, which is occupied by a hydrophobic ligand. This interaction is structurally reminiscent of the binding of a prenyl group by a regulatory protein, the Rho guanine nucleotide exchange inhibitor. The crystal structure suggests that binding of non-polar molecules may be essential to the physiological function of the Der p 2 protein.

Copyright 2002 Elsevier Science Ltd.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk