2fo4
From Proteopedia
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|PDB= 2fo4 |SIZE=350|CAPTION= <scene name='initialview01'>2fo4</scene>, resolution 2.70Å | |PDB= 2fo4 |SIZE=350|CAPTION= <scene name='initialview01'>2fo4</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1g7q|1G7Q]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fo4 OCA], [http://www.ebi.ac.uk/pdbsum/2fo4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fo4 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Lazoura, E.]] | [[Category: Lazoura, E.]] | ||
[[Category: Ramsland, P A.]] | [[Category: Ramsland, P A.]] | ||
| - | [[Category: MPD]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PO4]] | ||
[[Category: anchor modification]] | [[Category: anchor modification]] | ||
[[Category: h-2kb]] | [[Category: h-2kb]] | ||
| Line 34: | Line 34: | ||
[[Category: vaccine design]] | [[Category: vaccine design]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:26 2008'' |
Revision as of 00:05, 31 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1G7Q
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Enhanced MHC class I binding and immune responses through anchor modification of the non-canonical tumor associated MUC1-8 peptide
Overview
Designing peptide-based vaccines for therapeutic applications in cancer immunotherapy requires detailed knowledge of the interactions between the antigenic peptide and major histocompatibility complex (MHC) in addition to that between the peptide-MHC complex and the T-cell receptor. Past efforts to immunize with high-affinity tumour-associated antigenic peptides have not been very immunogenic, which may be attributed to the lack of T cells to these peptides, having been deleted during thymic development. For this reason, low-to-medium affinity non-canonical peptides represent more suitable candidates. However, in addition to the difficulty in identifying such antigens, peptide binding to MHC, and hence its ability to induce a strong immune response, is limited. Therefore, to enhance binding to MHC and improve immune responses, anchor modifications of non-canonical tumour-associated peptides would be advantageous. In this study, the non-canonical tumour-associated peptide from MUC1, MUC1-8 (SAPDTRPA), was modified at the MHC anchor residues to SAPDFRPL (MUC1-8-5F8L) and showed enhanced binding to H-2Kb and improved immune responses. Furthermore, the crystal structure of MUC1-8-5F8L in complex with H-2Kb was determined and it revealed that binding of the peptide to MHC is similar to that of the canonical peptide OVA8 (SIINFEKL).
About this Structure
2FO4 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Enhanced major histocompatibility complex class I binding and immune responses through anchor modification of the non-canonical tumour-associated mucin 1-8 peptide., Lazoura E, Lodding J, Farrugia W, Ramsland PA, Stevens J, Wilson IA, Pietersz GA, Apostolopoulos V, Immunology. 2006 Nov;119(3):306-16. PMID:17067310
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