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| [[Image:1i7t.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1i7t| PDB=1i7t | SCENE= }} | | {{STRUCTURE_1i7t| PDB=1i7t | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-5V'''
| | ===CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-5V=== |
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| ==Overview==
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| Recognition of virally infected cells by CD8+ T cells requires differentiation between self and nonself peptide-class I major histocompatibility complexes (pMHC). Recognition of foreign pMHC by host T cells is a major factor in the rejection of transplanted organs from the same species (allotransplant) or different species (xenotransplant). AHIII12.2 is a murine T cell clone that recognizes the xenogeneic (human) class I MHC HLA-A2.1 molecule (A2) and the syngeneic murine class I MHC H-2 D(b) molecule (D(b)). Recognition of both A2 and D(b) are peptide-dependent, and the sequences of the peptides recognized have been determined. Alterations in the antigenic peptides bound to A2 cause large changes in AHIII12.2 T cell responsiveness. Crystal structures of three representative peptides (agonist, null, and antagonist) bound to A2 partially explain the changes in AHIII12.2 responsiveness. Using class I pMHC octamers, a strong correlation is seen between T cell activity and the affinity of pMHC complexes for the T cell receptor. However, contrary to previous studies, we see similar half-lives for the pMHC multimers bound to the AHIII12.2 cell surface.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11584024}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11584024 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11584024}} |
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| ==Disease== | | ==Disease== |
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| [[Category: Zhao, R.]] | | [[Category: Zhao, R.]] |
| [[Category: Mhc fold]] | | [[Category: Mhc fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:40:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:32:56 2008'' |
