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| Article Authors: | C R Wang; A R Castaño; P A Peterson; C Slaughter; K F Lindahl; J Deisenhofer |
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| Article Title: | Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3. |
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| Reference ID: | 1013618 |
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| Abstract: | H2-M3 is a class Ib MHC molecule of the mouse with a 10(4)-fold preference for binding N-formylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a formylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray crystallography. M3, refined at 2.1 A resolution, resembles class la MHC molecules in its overall structure, but differs in the peptide-binding groove. The A pocket, which usually accommodates the free N-terminus of a bound peptide, is closed, and the peptide is shifted one residue, such that the P1 side chain is lodged in the B pocket. The formyl group is coordinated by His-9 and a bound water on the floor of the groove. |
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| Affiliations: | Department of Biochemistry, University of Texas Southwestern Medical Center Dallas 75235-9050, USA. |
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| Date: | 1995 |
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| Reference Type: | Literature |
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| PubMed ID: | 7664344 |
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| Journal: | Cell |
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| Journal Volume: | 82 |
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| Article Pages: | 655-64 |
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| Journal ISSN: | 0092-8674 |
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| Article Chemical List: | DNA, Complementary;Histocompatibility Antigens Class I;Oligopeptides;N-Formylmethionine |
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| Article MeSH List: | Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA, Complementary(genetics); Electrochemistry; Histocompatibility Antigens Class I(chemistry; genetics; metabolism); Mice; Models, Molecular; Molecular Sequence Data; Molecular Structure; N-Formylmethionine(metabolism); Oligopeptides(chemistry; genetics; metabolism); Protein Binding; Protein Conformation |
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| Curation Last Updated: | 2010-09-11 20:01:10 |
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