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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 DOI10.2210/pdb1jf1/pdb
Related1JHT
DescriptorHLA 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 Keywordshuman, tumor immunity, melanoma antigen, mhc, vaccination, melanoma, class i, immune system
Biological sourceHomo sapiens (human)
More
Cellular locationMembrane; Single-pass type I membrane protein: P01892
Secreted: P61769
Total number of polymer chains3
Total formula weight44784.14
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 citationSliz, 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: 11544315
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

226707

數據於2024-10-30公開中

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