Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The crystal structure of a major dust mite allergen Der p 2, and its biological implications.,Derewenda U, Li J, Derewenda Z, Dauter Z, Mueller GA, Rule GS, Benjamin DC J Mol Biol. 2002 Apr 19;318(1):189-97. PMID:12054778[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Derewenda U, Li J, Derewenda Z, Dauter Z, Mueller GA, Rule GS, Benjamin DC. The crystal structure of a major dust mite allergen Der p 2, and its biological implications. J Mol Biol. 2002 Apr 19;318(1):189-97. PMID:12054778 doi:http://dx.doi.org/10.1016/S0022-2836(02)00027-X