1AQD

HLA-DR1 (DRA, DRB1 0101) HUMAN CLASS II HISTOCOMPATIBILITY PROTEIN (EXTRACELLULAR DOMAIN) COMPLEXED WITH ENDOGENOUS PEPTIDE

Summary for 1AQD

• Entry DOI: 10.2210/pdb1aqd/pdb
• Descriptor: HLA-DR1 CLASS II HISTOCOMPATIBILITY PROTEIN, HLA-A2, ... (4 entities in total)
• Functional Keywords: complex (mhc protein-antigen), histocompatibility antigen, complex (mhc protein-antigen) complex, complex (mhc protein/antigen)
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: P01903 P04229; Membrane; Single-pass type I membrane protein: P01892
• Total number of polymer chains: 12
• Total formula weight: 188146.67

Authors

Murthy, V.L.,Stern, L.J. (deposition date: 1997-07-28, release date: 1998-01-28, Last modification date: 2023-08-02)

Primary citation

Murthy, V.L.,Stern, L.J.
The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding.
Structure, 5:1385-1396, 1997

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.

PubMed: 9351812
DOI: 10.1016/S0969-2126(97)00288-8

Experimental method

X-RAY DIFFRACTION (2.45 Å)