Title

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

Date of Original Version

4-19-2002

Type

Article

PubMed ID

12054778

Abstract or Description

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.

DOI

10.1016/S0022-2836(02)00027-X

 

Published In

Journal of molecular biology, 318, 1, 189-197.