1i7u
From Proteopedia
(New page: 200px<br /> <applet load="1i7u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i7u, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF...) |
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caption="1i7u, resolution 1.8Å" /> | caption="1i7u, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-6V'''<br /> | '''CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-6V'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I7U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1I7U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: mhc fold]] | [[Category: mhc fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:59:50 2008'' |
Revision as of 13:59, 15 February 2008
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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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