2fo4: Difference between revisions

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[[Image:2fo4.gif|left|200px]]<br /><applet load="2fo4" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2fo4.gif|left|200px]]
caption="2fo4, resolution 2.70&Aring;" />
 
'''Enhanced MHC class I binding and immune responses through anchor modification of the non-canonical tumor associated MUC1-8 peptide'''<br />
{{Structure
|PDB= 2fo4 |SIZE=350|CAPTION= <scene name='initialview01'>2fo4</scene>, resolution 2.70&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
|ACTIVITY=
|GENE=
}}
 
'''Enhanced MHC class I binding and immune responses through anchor modification of the non-canonical tumor associated MUC1-8 peptide'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2FO4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FO4 OCA].  
2FO4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FO4 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17067310 17067310]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17067310 17067310]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: NAG]]
[[Category: NAG]]
[[Category: PO4]]
[[Category: PO4]]
[[Category: anchor modifications]]
[[Category: anchor modification]]
[[Category: h-2kb]]
[[Category: h-2kb]]
[[Category: muc1]]
[[Category: muc1]]
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[[Category: vaccine design]]
[[Category: vaccine design]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:23 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:47 2008''

Revision as of 14:54, 20 March 2008

File:2fo4.gif


Drag the structure with the mouse to rotate
2fo4, resolution 2.70Å
Ligands: NAG, PO4 and MPD
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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