| Literature DB >> 12734347 |
Adrian Davies1, Suzanne Kalb, Bitao Liang, Carla J Aldrich, François A Lemonnier, Hong Jiang, Robert Cotter, Mark J Soloski.
Abstract
The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class Ia proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change.Entities:
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Year: 2003 PMID: 12734347 DOI: 10.4049/jimmunol.170.10.5027
Source DB: PubMed Journal: J Immunol ISSN: 0022-1767 Impact factor: 5.422