1TMC

THE THREE-DIMENSIONAL STRUCTURE OF A CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE MISSING THE ALPHA3 DOMAIN OF THE HEAVY CHAIN

Summary for 1TMC

• Entry DOI: 10.2210/pdb1tmc/pdb
• Descriptor: CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-AW68), BETA 2-MICROGLOBULIN, DECAMERIC PEPTIDE (EVAPPEYHRK), ... (4 entities in total)
• Functional Keywords: histocompatibility antigen
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01891; Secreted: P61769
• Total number of polymer chains: 3
• Total formula weight: 33423.07

Authors

Collins, E.J.,Garboczi, D.N.,Karpusas, M.N.,Wiley, D.C. (deposition date: 1994-12-19, release date: 1995-03-31, Last modification date: 2024-10-30)

Primary citation

Collins, E.J.,Garboczi, D.N.,Karpusas, M.N.,Wiley, D.C.
The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain.
Proc.Natl.Acad.Sci.USA, 92:1218-1221, 1995

PubMed Abstract: Class I major histocompatibility complex (MHC) molecules are ternary complexes of the soluble serum protein beta 2-microglobulin, MHC heavy chain, and bound peptide. The first two domains (alpha 1, alpha 2) of the heavy chain create the peptide binding cleft and the surface that contacts the T-cell receptor. The third domain (alpha 3) associates with the T-cell co-receptor, CD8, during T-cell recognition. Here we describe the x-ray crystal structure of a human class I MHC molecule, HLA-Aw68, from which the alpha 3 domain has been proteolytically removed. The resulting molecule shows no gross morphological changes compared to the intact protein. A decameric peptide complexed with the intact HLA-Aw68 is seen to bind to the proteolized molecule in the conventional manner, demonstrating that the alpha 3 domain is not required for the structural integrity of the molecule or for peptide binding.

PubMed: 7862664
DOI: 10.1073/pnas.92.4.1218

Experimental method

X-RAY DIFFRACTION (2.3 Å)