1KTJ

X-ray Structure Of Der P 2, The Major House Dust Mite Allergen

Summary for 1KTJ

• Entry DOI: 10.2210/pdb1ktj/pdb
• Descriptor: ALLERGEN DER P 2 (2 entities in total)
• Functional Keywords: allergen, asthma, immunoglobulin fold, hydrophobic cavity
• Biological source: Dermatophagoides pteronyssinus (European house dust mite)
• Cellular location: Secreted: P49278
• Total number of polymer chains: 2
• Total formula weight: 28230.64

Authors

Derewenda, U.,Li, J.,Derewenda, Z.,Dauter, Z.,Mueller, G.A.,Rule, G.S.,Benjamin, D.C. (deposition date: 2002-01-16, release date: 2002-05-15, Last modification date: 2024-11-20)

Primary citation

Derewenda, U.,Li, J.,Derewenda, Z.,Dauter, Z.,Mueller, G.A.,Rule, G.S.,Benjamin, D.C.
The crystal structure of a major dust mite allergen Der p 2, and its biological implications.
J.Mol.Biol., 318:189-197, 2002

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.

PubMed: 12054778
DOI: 10.1016/S0022-2836(02)00027-X

Experimental method

X-RAY DIFFRACTION (2.15 Å)