The Structure and Stability of the Monomorphic HLA-G Are Influenced by the Nature of the Bound Peptide
Nicholas G Walpole, Lars Kjer-Nielsen, Lyudmila Kostenko, James McCluskey, Andrew G Brooks, Jamie Rossjohn, Craig S Clements
JOURNAL OF MOLECULAR BIOLOGY | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2010
The highly polymorphic major histocompatibility complex class Ia (MHC-Ia) molecules present a broad array of peptides to the clonotypically diverse alphabeta T-cell receptors. In contrast, MHC-Ib molecules exhibit limited polymorphism and bind a more restricted peptide repertoire, in keeping with their major role in innate immunity. Nevertheless, some MHC-Ib molecules do play a role in adaptive immunity. While human leukocyte antigen E (HLA-E), the MHC-Ib molecule, binds a very restricted repertoire of peptides, the peptide binding preferences of HLA-G, the class Ib molecule, are less stringent, although the basis by which HLA-G can bind various peptides is unclear. To investigate how HLA-G ..View full abstract
Awarded by NATIONAL CENTER FOR RESEARCH RESOURCES
The National Health and Medical Research Council and the Australian Research Council (ARC) supported this work. J.R. is supported by an ARC Federation Fellowship, and C.S.C. is supported by an ARC Queen Elizabeth H Fellowship. We thank the staff at the BioCARS and GM/CA-CAT for their assistance with data collection.