1e28
From Proteopedia
(New page: 200px<br /> <applet load="1e28" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e28, resolution 3.0Å" /> '''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. | ||
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| + | ==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 16:38:51 2007'' |
Revision as of 14:32, 12 November 2007
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NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2(TAFTIPSI)
Contents |
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.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]
About this Structure
1E28 is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Nonstandard peptide binding revealed by crystal structures of HLA-B*5101 complexed with HIV immunodominant epitopes., Maenaka K, Maenaka T, Tomiyama H, Takiguchi M, Stuart DI, Jones EY, J Immunol. 2000 Sep 15;165(6):3260-7. PMID:10975842
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