1JHT

Crystal structure of HLA-A2*0201 in complex with a nonameric altered peptide ligand (ALGIGILTV) from the MART-1/Melan-A.

Summary for 1JHT

• Entry DOI: 10.2210/pdb1jht/pdb
• Related: 1JF1
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN, beta-2-microglobulin, nonameric peptide ligand from the MART-1/Melan-A, ... (4 entities in total)
• Functional Keywords: human, tumor immunity, melanoma antigen, mhc, vaccination, melanoma, class i, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted: P61769
• Total number of polymer chains: 3
• Total formula weight: 44589.62

Authors

Sliz, P.,Michielin, O.,Karplus, M.,Romero, P.,Wiley, D. (deposition date: 2001-06-28, release date: 2001-09-14, Last modification date: 2024-10-30)

Primary citation

Sliz, P.,Michielin, O.,Cerottini, J.C.,Luescher, I.,Romero, P.,Karplus, M.,Wiley, D.C.
Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes.
J.Immunol., 167:3276-3284, 2001

PubMed Abstract: We have determined high-resolution crystal structures of the complexes of HLA-A2 molecules with two modified immunodominant peptides from the melanoma tumor-associated protein Melan-A/Melanoma Ag recognized by T cells-1. The two peptides, a decamer and nonamer with overlapping sequences (ELAGIGILTV and ALGIGILTV), are modified in the second residue to increase their affinity for HLA-A2. The modified decamer is more immunogenic than the natural peptide and a candidate for peptide-based melanoma immunotherapy. The crystal structures at 1.8 and 2.15 A resolution define the differences in binding modes of the modified peptides, including different clusters of water molecules that appear to stabilize the peptide-HLA interaction. The structures suggest both how the wild-type peptides would bind and how three categories of cytotoxic T lymphocytes with differing fine specificity might recognize the two peptides.

PubMed: 11544315

Experimental method

X-RAY DIFFRACTION (2.15 Å)