1lp9
From Proteopedia
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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
Page seeded by OCA on Mon Nov 12 18:03:00 2007
