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- Title
Recognition surfaces of MHC class I.
- Authors
Jones, E. Yvonne; Tormo, Jose; Reid, Scott W.; Stuart, David I.
- Abstract
Recent crystallographic results have provided close to atomicresolution views of the recognition events mediated by MHC class I molecules. The specificity-conferring interaction of MHC class I/peptide with a T-cell antigen receptor (TCR) appears dependent on certain key interactions with the MHC scaffold. These interactions, in particular those of the TCR Vα domain, define a standard orientation for TCR binding. Previous studies on biologically significant variations in the TCR recognition surface presented by a series of MHC/variant peptide complexes can be reassessed in the light of this TCR-binding mode. The interaction of CD8 with MHC class I resembles that between antibody and antigen in the use of loops from the CD8 structure. The interaction is of very low affinity and buries equivalent surface area to that between the TCR and MHC class I but while the TCR/MHC interface shows poor surface shape complementarity the match in the conservative interaction between MHC and CD8 is precise.
- Subjects
ANTIGENS; PEPTIDES
- Publication
Immunological Reviews, 1998, Vol 163, Issue 1, p121
- ISSN
0105-2896
- Publication type
Article
- DOI
10.1111/j.1600-065X.1998.tb01191.x