1lp9

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(New page: 200px<br /> <applet load="1lp9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lp9, resolution 2.00&Aring;" /> '''Xenoreactive comple...)
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[[Image:1lp9.gif|left|200px]]<br />
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<applet load="1lp9" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1lp9, resolution 2.00&Aring;" />
caption="1lp9, resolution 2.00&Aring;" />
'''Xenoreactive complex AHIII 12.2 TCR bound to p1049/HLA-A2.1'''<br />
'''Xenoreactive complex AHIII 12.2 TCR bound to p1049/HLA-A2.1'''<br />
==Overview==
==Overview==
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T cell receptors (TCR) adopt a similar orientation when binding with major, histocompatibility complex (MHC) molecules, yet the biological mechanism, that generates this similar TCR orientation remains obscure. We show here, the cocrystallographic structure of a mouse TCR bound to a human MHC, molecule not seen by the TCR during thymic development. The orientation of, this xenoreactive murine TCR atop human MHC deviates from the typical, orientation more than any previously determined TCR/MHC structure. This, unique orientation is solely due to the placement of the TCR Valpha domain, on the MHC. In light of new information provided by this structure, we, have reanalyzed the existing TCR/MHC cocrystal structures and discovered, unique features of TCR Valpha domain position on class I MHC that, correlate with CD8 dependence. Finally, we propose that the orientation, seen in TCR recognition of MHC is a consequence of selection during T cell, development.
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T cell receptors (TCR) adopt a similar orientation when binding with major histocompatibility complex (MHC) molecules, yet the biological mechanism that generates this similar TCR orientation remains obscure. We show here the cocrystallographic structure of a mouse TCR bound to a human MHC molecule not seen by the TCR during thymic development. The orientation of this xenoreactive murine TCR atop human MHC deviates from the typical orientation more than any previously determined TCR/MHC structure. This unique orientation is solely due to the placement of the TCR Valpha domain on the MHC. In light of new information provided by this structure, we have reanalyzed the existing TCR/MHC cocrystal structures and discovered unique features of TCR Valpha domain position on class I MHC that correlate with CD8 dependence. Finally, we propose that the orientation seen in TCR recognition of MHC is a consequence of selection during T cell development.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1LP9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LP9 OCA].
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1LP9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LP9 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Appella, E.]]
[[Category: Appella, E.]]
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[[Category: Biddison, W.E.]]
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[[Category: Biddison, W E.]]
[[Category: Buslepp, J.]]
[[Category: Buslepp, J.]]
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[[Category: Collins, E.J.]]
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[[Category: Collins, E J.]]
[[Category: Wang, H.]]
[[Category: Wang, H.]]
[[Category: class i mhc:tcr co-crystal]]
[[Category: class i mhc:tcr co-crystal]]
[[Category: immunoregulatory complex]]
[[Category: immunoregulatory complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:03:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:04 2008''

Revision as of 11:47, 21 February 2008


1lp9, resolution 2.00Å

Drag the structure with the mouse to rotate

Xenoreactive complex AHIII 12.2 TCR bound to p1049/HLA-A2.1

Contents

Overview

T cell receptors (TCR) adopt a similar orientation when binding with major histocompatibility complex (MHC) molecules, yet the biological mechanism that generates this similar TCR orientation remains obscure. We show here the cocrystallographic structure of a mouse TCR bound to a human MHC molecule not seen by the TCR during thymic development. The orientation of this xenoreactive murine TCR atop human MHC deviates from the typical orientation more than any previously determined TCR/MHC structure. This unique orientation is solely due to the placement of the TCR Valpha domain on the MHC. In light of new information provided by this structure, we have reanalyzed the existing TCR/MHC cocrystal structures and discovered unique features of TCR Valpha domain position on class I MHC that correlate with CD8 dependence. Finally, we propose that the orientation seen in TCR recognition of MHC is a consequence of selection during T cell development.

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

1LP9 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

A correlation between TCR Valpha docking on MHC and CD8 dependence: implications for T cell selection., Buslepp J, Wang H, Biddison WE, Appella E, Collins EJ, Immunity. 2003 Oct;19(4):595-606. PMID:14563323

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