The crystal structure of a major dust mite allergen Der p 2, and its biological implications.
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.
Derewenda
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Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA. ud3a@virginia.edu
Li
J
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Derewenda
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Dauter
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Mueller
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Rule
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Benjamin
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D000485:Allergens / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D039741:Antigens, Dermatophagoides; D003460:Crystallization; D004220:Disulfides / Q000737:chemistry; D004391:Dust; D000939:Epitopes; D004926:Escherichia coli / Q000235:genetics; D006023:Glycoproteins; D006860:Hydrogen Bonding; D007136:Immunoglobulins / Q000737:chemistry; D008024:Ligands; D008715:Methionine / Q000737:chemistry; D008925:Mites; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012643:Selenium / Q000737:chemistry; D014867:Water / Q000737:chemistry
D000485:Allergens; D039741:Antigens, Dermatophagoides; D004220:Disulfides; D004391:Dust; D000939:Epitopes; D006023:Glycoproteins; D007136:Immunoglobulins; D008024:Ligands; D011994:Recombinant Proteins; D014867:Water; D008715:Methionine; D012643:Selenium