5a2j
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a2j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a2j RCSB], [http://www.ebi.ac.uk/pdbsum/5a2j PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a2j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a2j RCSB], [http://www.ebi.ac.uk/pdbsum/5a2j PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The structural features of MUC1-like glycopeptides bearing the Tn antigen (alpha-O-GalNAc-Ser/Thr) in complex with an anti MUC-1 antibody are reported at atomic resolution. For the alpha-O-GalNAc-Ser derivative, the glycosidic linkage adopts a high-energy conformation, barely populated in the free state. This unusual structure (also observed in an alpha-S-GalNAc-Cys mimic) is stabilized by hydrogen bonds between the peptidic fragment and the sugar. The selection of a particular peptide structure by the antibody is thus propagated to the carbohydrate through carbohydrate/peptide contacts, which force a change in the orientation of the sugar moiety. This seems to be unfeasible in the alpha-O-GalNAc-Thr glycopeptide owing to the more limited flexibility of the side chain imposed by the methyl group. Our data demonstrate the non-equivalence of Ser and Thr O-glycosylation points in molecular recognition processes. These features provide insight into the occurrence in nature of the APDTRP epitope for anti-MUC1 antibodies. | ||
+ | |||
+ | Deciphering the Non-Equivalence of Serine and Threonine O-Glycosylation Points: Implications for Molecular Recognition of the Tn Antigen by an anti-MUC1 Antibody.,Martinez-Saez N, Castro-Lopez J, Valero-Gonzalez J, Madariaga D, Companon I, Somovilla VJ, Salvado M, Asensio JL, Jimenez-Barbero J, Avenoza A, Busto JH, Bernardes GJ, Peregrina JM, Hurtado-Guerrero R, Corzana F Angew Chem Int Ed Engl. 2015 Jun 26. doi: 10.1002/anie.201502813. PMID:26118689<ref>PMID:26118689</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 08:26, 8 July 2015
Crystal structure of scFv-SM3 in complex with the naked peptide APDTRP
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Categories: Asensio, J L | Avenoza, A | Bernardes, G J.L | Busto, J H | Castro-Lopez, J | Companon, I | Corzana, F | Hurtado-Guerrero, R | Jimenez-Barbero, J | Madariaga, D | Martinez-Saez, N | Peregrina, J M | Salvado, M | Somovilla, V J | Valero-Gonzalez, J | Antibody | Conformation analysis | Fusion protein | Glycopeptide | Molecular recognition | Peptide binding protein