1ktj
From Proteopedia
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'''X-ray Structure Of Der P 2, The Major House Dust Mite Allergen''' | '''X-ray Structure Of Der P 2, The Major House Dust Mite Allergen''' | ||
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[[Category: Mueller, G A.]] | [[Category: Mueller, G A.]] | ||
[[Category: Rule, G S.]] | [[Category: Rule, G S.]] | ||
| - | [[Category: | + | [[Category: Allergen]] |
| - | [[Category: | + | [[Category: Asthma]] |
| - | [[Category: | + | [[Category: Hydrophobic cavity]] |
| - | [[Category: | + | [[Category: Immunoglobulin fold]] |
| - | [[Category: | + | [[Category: X-ray structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:09:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:09, 2 May 2008
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 Page seeded by OCA on Fri May 2 23:09:17 2008
