1i7u

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==Overview==
==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.
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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.
==Disease==
==Disease==
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[[Category: Appella, E.]]
[[Category: Appella, E.]]
[[Category: Busslep, J.]]
[[Category: Busslep, J.]]
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[[Category: Collins, E.J.]]
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[[Category: Collins, E J.]]
[[Category: Loftus, D.]]
[[Category: Loftus, D.]]
[[Category: Zhao, R.]]
[[Category: Zhao, R.]]
[[Category: mhc fold]]
[[Category: mhc fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:59:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:56 2008''

Revision as of 11:08, 21 February 2008


1i7u, resolution 1.8Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-6V

Contents

Overview

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.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]

About this Structure

1I7U is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

T cell activity correlates with oligomeric peptide-major histocompatibility complex binding on T cell surface., Buslepp J, Zhao R, Donnini D, Loftus D, Saad M, Appella E, Collins EJ, J Biol Chem. 2001 Dec 14;276(50):47320-8. Epub 2001 Oct 2. PMID:11584024

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