1e27: Difference between revisions
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New page: left|200px<br /> <applet load="1e27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e27, resolution 2.2Å" /> '''NONSTANDARD PEPTIDE ... |
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==Overview== | ==Overview== | ||
The crystal structures of the human MHC class I allele HLA-B*5101 in, complex with 8-mer, TAFTIPSI, and 9-mer, LPPVVAKEI, immunodominant peptide, epitopes from HIV-1 have been determined by x-ray crystallography. In both, complexes, the hydrogen-bonding network in the N-terminal anchor (P1), pocket is rearranged as a result of the replacement of the standard, tyrosine with histidine at position 171. This results in a nonstandard, positioning of the peptide N terminus, which is recognized by, B*5101-restricted T cell clones. Unexpectedly, the P5 peptide residues, appear to act as anchors, drawing the peptides unusually deeply into the, peptide-binding groove of B51. The unique characteristics of P1 and P5 are, likely to be responsible for the zig-zag conformation of the 9-mer peptide, and the slow assembly of B*5101. A comparison of the surface, characteristics in the alpha1-helix C-terminal region for B51 and other, MHC class I alleles highlights mainly electrostatic differences that may, be important in determining the specificity of human killer cell Ig-like, receptor binding. | The crystal structures of the human MHC class I allele HLA-B*5101 in, complex with 8-mer, TAFTIPSI, and 9-mer, LPPVVAKEI, immunodominant peptide, epitopes from HIV-1 have been determined by x-ray crystallography. In both, complexes, the hydrogen-bonding network in the N-terminal anchor (P1), pocket is rearranged as a result of the replacement of the standard, tyrosine with histidine at position 171. This results in a nonstandard, positioning of the peptide N terminus, which is recognized by, B*5101-restricted T cell clones. Unexpectedly, the P5 peptide residues, appear to act as anchors, drawing the peptides unusually deeply into the, peptide-binding groove of B51. The unique characteristics of P1 and P5 are, likely to be responsible for the zig-zag conformation of the 9-mer peptide, and the slow assembly of B*5101. A comparison of the surface, characteristics in the alpha1-helix C-terminal region for B51 and other, MHC class I alleles highlights mainly electrostatic differences that may, be important in determining the specificity of human killer cell Ig-like, receptor binding. | ||
==Disease== | |||
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Spondyloarthropathy, susceptibility to, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: mhc class i]] | [[Category: mhc class i]] | ||
''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 16:38:49 2007'' | ||
