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PDBsum entry 5a2k
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Immune system
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PDB id
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5a2k
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References listed in PDB file
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Key reference
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Title
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Deciphering the non-Equivalence of serine and threonine o-Glycosylation points: implications for molecular recognition of the tn antigen by an anti-Muc1 antibody.
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Authors
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N.Martínez-Sáez,
J.Castro-López,
J.Valero-González,
D.Madariaga,
I.Compañón,
V.J.Somovilla,
M.Salvadó,
J.L.Asensio,
J.Jiménez-Barbero,
A.Avenoza,
J.H.Busto,
G.J.Bernardes,
J.M.Peregrina,
R.Hurtado-Guerrero,
F.Corzana.
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Ref.
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Angew Chem Int Ed Engl, 2015,
54,
9830-9834.
[DOI no: ]
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PubMed id
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Abstract
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The structural features of MUC1-like glycopeptides bearing the Tn antigen
(α-O-GalNAc-Ser/Thr) in complex with an anti MUC-1 antibody are reported at
atomic resolution. For the α-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 α-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
α-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.
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