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J. Biol. Chem., Vol. 275, Issue 21, 16098-16102, May 26, 2000
From the Structural Biology Unit, National Institute of Immunology,
Aruna Asaf Ali Marg, New Delhi 110 067, India
The functional consequences of
peptide-carbohydrate mimicry were analyzed on the basis of the crystal
structure of concanavalin A (ConA) in complex with a
carbohydrate-mimicking peptide, DVFYPYPYASGS. The peptide binds to the
non-crystallographically related monomers of two independent dimers of
ConA in two different modes, in slightly different conformations,
demonstrating structural adaptability in ConA-peptide recognition. In
one mode, the peptide has maximum interactions with ConA, and in the
other, it shows relatively fewer contacts within this site but
significant contacts with the symmetry-related subunit. Neither of the
peptide binding sites overlaps with the structurally characterized
mannose and trimannose binding sites on ConA. Despite this, the
functional mimicry between the peptide and carbohydrate ligands was
evident. The peptide-inhibited ConA induced T cell proliferation in a
dose-dependent manner. The effect of the designed analogs
of the peptide on ConA-induced T cell proliferation and their
recognition by the antibody response against
Structural and Functional Consequences of Peptide-Carbohydrate
Mimicry
CRYSTAL STRUCTURE OF A CARBOHYDRATE-MIMICKING PEPTIDE BOUND TO
CONCANAVALIN A*
,
-D-mannopyranoside indicate a role for aromatic
residues in functional mimicry. Although the functional mimicry was
observed between the peptide and carbohydrate moieties, the crystal
structure of the ConA-peptide complex revealed that the two peptide
binding sites are independent of the methyl
-D-mannopyranoside binding site.
*
This work was supported by the Department of Biotechnology
(GOI) with funds provided to National Institute of Immunology.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of the fellowship from the CSIR (India).
§
To whom correspondence should be addressed. Tel.: 91 11 616 7623 (ext. 234); Fax: 91 11 616 2125; E-mail: dinakar@nii.res.in.
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