1JF1
Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A
Summary for 1JF1
Entry DOI | 10.2210/pdb1jf1/pdb |
Related | 1JHT |
Descriptor | HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN, beta-2-microglobulin, decameric peptide ligand from the MART-1/Melan-A, ... (5 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 | 44784.14 |
Authors | Sliz, P.,Michielin, O.,Cerottini, J.C.,Luescher, I.,Romero, P.,Karplus, M.,Wiley, D.C. (deposition date: 2001-06-19, release date: 2001-09-14, Last modification date: 2024-10-16) |
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 Cited by 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: 11544315PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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