1ktj

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1ktj, resolution 2.15Å

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

Overview

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.

About this Structure

1KTJ is a Single protein structure of sequence from Dermatophagoides pteronyssinus. Full crystallographic information is available from OCA.

Reference

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

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