1ktj
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ktj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktj OCA], [http://www.ebi.ac.uk/pdbsum/1ktj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ktj RCSB]</span> | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:21 2008'' |
Revision as of 18:53, 30 March 2008
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| , resolution 2.15Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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