1jf1: Difference between revisions
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|PDB= 1jf1 |SIZE=350|CAPTION= <scene name='initialview01'>1jf1</scene>, resolution 1.85Å | |PDB= 1jf1 |SIZE=350|CAPTION= <scene name='initialview01'>1jf1</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1jht|1JHT]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jf1 OCA], [http://www.ebi.ac.uk/pdbsum/1jf1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jf1 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Sliz, P.]] | [[Category: Sliz, P.]] | ||
[[Category: Wiley, D C.]] | [[Category: Wiley, D C.]] | ||
[[Category: class i]] | [[Category: class i]] | ||
[[Category: human]] | [[Category: human]] | ||
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[[Category: vaccination]] | [[Category: vaccination]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:46 2008'' | ||