1LP9

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

Summary for 1LP9

• Entry DOI: 10.2210/pdb1lp9/pdb
• Descriptor: HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, self-peptide P1049, ... (6 entities in total)
• Functional Keywords: immunoregulatory complex, class i mhc:tcr co-crystal, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted: P61769
• Total number of polymer chains: 10
• Total formula weight: 186660.05

Authors

Buslepp, J.,Wang, H.,Biddison, W.E.,Appella, E.,Collins, E.J. (deposition date: 2002-05-07, release date: 2003-11-11, Last modification date: 2023-09-20)

Primary citation

Buslepp, J.,Wang, H.,Biddison, W.E.,Appella, E.,Collins, E.J.
A correlation between TCR Valpha docking on MHC and CD8 dependence: implications for T cell selection.
Immunity, 19:595-606, 2003

PubMed Abstract: 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.

PubMed: 14563323
DOI: 10.1016/S1074-7613(03)00269-3

Experimental method

X-RAY DIFFRACTION (2 Å)