1hhg: Difference between revisions
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New page: left|200px<br /> <applet load="1hhg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hhg, resolution 2.6Å" /> '''THE ANTIGENIC IDENTI... |
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==Overview== | ==Overview== | ||
Complexes of five peptides (from HIV-1, influenza A virus, HTLV-1, and, hepatitis B virus proteins) bound to the human class I MHC molecule HLA-A2, have been studied by X-ray crystallography. While the peptide termini and, their second and C-terminal anchor side chains are bound similarly in all, five cases, the main chain and side chain conformations of each peptide, are strikingly different in the center of the binding site, and these, differences are accessible to direct TCR recognition. Each of the central, peptide residues is seen to point up for some bound peptides, but down or, sideways for others. Thus, although fixed at its ends, the structure of an, MHC-bound peptide appears to be a highly complex function of its entire, sequence, potentially sensitive to even small sequence differences. In, contrast, MHC structural variation is relatively limited. These results, offer a structural framework for understanding the role of nonanchor, peptide side chains in both peptide-MHC binding affinity and TCR, recognition. | Complexes of five peptides (from HIV-1, influenza A virus, HTLV-1, and, hepatitis B virus proteins) bound to the human class I MHC molecule HLA-A2, have been studied by X-ray crystallography. While the peptide termini and, their second and C-terminal anchor side chains are bound similarly in all, five cases, the main chain and side chain conformations of each peptide, are strikingly different in the center of the binding site, and these, differences are accessible to direct TCR recognition. Each of the central, peptide residues is seen to point up for some bound peptides, but down or, sideways for others. Thus, although fixed at its ends, the structure of an, MHC-bound peptide appears to be a highly complex function of its entire, sequence, potentially sensitive to even small sequence differences. In, contrast, MHC structural variation is relatively limited. These results, offer a structural framework for understanding the role of nonanchor, peptide side chains in both peptide-MHC binding affinity and TCR, recognition. | ||
==Disease== | |||
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]], Ankylosing spondylitis, susceptibility to, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Stevens-Johnson syndrome, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:17:58 2007'' | ||
