Download MendeleyThe crystal structure of a major dust mite allergen Der p 2, and its biological implications.
Derewenda, U., Li, J., Derewenda, Z., Dauter, Z., Mueller, G.A., Rule, G.S., Benjamin, D.C.(2002) J Mol Biol 318: 189-197
- PubMed: 12054778
- DOI: https://doi.org/10.1016/S0022-2836(02)00027-X
- Primary Citation of Related Structures:
1KTJ - PubMed 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.
Organizational Affiliation:
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA. [email protected]
