The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding.
Murthy, V.L., Stern, L.J.(1997) Structure 5: 1385-1396
- PubMed: 9351812 
- DOI: https://doi.org/10.1016/s0969-2126(97)00288-8
- Primary Citation of Related Structures:  
1AQD - PubMed Abstract: 
Class II major histocompatibility complex (MHC) proteins are cell surface glycoproteins that bind peptides and present them to T cells as part of the mechanism for detecting and responding to foreign material in the body. The peptide-binding activity exhibits allele-specific preferences for particular sidechains at some positions, although the structural basis of these preferences is not understood in detail. We have determined the 2.45 A crystal structure of the human class II MHC protein HLA-DR1 in complex with the tight binding endogenous peptide A2 (103-117) in order to discover peptide-MHC interactions that are important in determining the binding motif and to investigate conformational constraints on the bound peptide.
Organizational Affiliation: 
Johns Hopkins University School of Medicine, Baltimore, MD 21210, USA.