1jf1
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Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]
About this StructureAbout this Structure
1JF1 is a Protein complex structure of sequences from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes., Sliz P, Michielin O, Cerottini JC, Luescher I, Romero P, Karplus M, Wiley DC, J Immunol. 2001 Sep 15;167(6):3276-84. PMID:11544315
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