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1i7t
From Proteopedia
(New page: 200px<br /> <applet load="1i7t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i7t, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1i7t.gif|left|200px]]<br /> | + | [[Image:1i7t.gif|left|200px]]<br /><applet load="1i7t" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1i7t" size=" | + | |
caption="1i7t, resolution 2.8Å" /> | caption="1i7t, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-5V'''<br /> | '''CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-5V'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Recognition of virally infected cells by CD8+ T cells requires | + | 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== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1I7T 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:// | + | 1I7T 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=1I7T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Appella, E.]] | [[Category: Appella, E.]] | ||
[[Category: Busslep, J.]] | [[Category: Busslep, J.]] | ||
| - | [[Category: Collins, E | + | [[Category: Collins, E J.]] |
[[Category: Loftus, D.]] | [[Category: Loftus, D.]] | ||
[[Category: Zhao, R.]] | [[Category: Zhao, R.]] | ||
[[Category: mhc fold]] | [[Category: mhc fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:53 2008'' |
Revision as of 11:08, 21 February 2008
|
CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-5V
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
1I7T 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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