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Structural basis of functional mimicry between carbohydrate and peptide ligands of con A.

Abstract：

:Crystallographic studies have shown independent binding sites for sugar and peptide ligands of concanavalin A, although they were considered functional mimics based on biochemical experiments. The topological correlation of 12-residue peptide with different carbohydrate ligands of concanavalin A showed similarity between trimannose and the YPY region of the peptide establishing structural mimicry. Molecular docking of trimannose and the YPY motif on the reciprocal binding sites revealed equivalent interactions and energetics implying that the peptide-binding sites may constitute additional sugar-binding subsites of concanavalin A. The binding of a mannose-rich neoglycoprotein with significantly higher affinity compared with that of the methyl alpha-d-mannopyranoside is consistent with this interpretation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Jain D,Kaur KJ,Goel M,Salunke DM

doi

10.1006/bbrc.2000.2871

subject

Has Abstract

pub_date

2000-06-16 00:00:00

pages

843-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92871-7

journal_volume

272

pub_type

杂志文章

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