Binding of nonpolar molecules by crystalline concanavalin A

Hardman, Karl D.; Ainsworth, Clinton F.

doi:10.1021/bi00746a022

Cited by 86 publications

(35 citation statements)

References 7 publications

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“…The interactions in this case are dominantly hydrophobic, involving aromatic residues in addition to hydrogen bonds. However, the peptide binding sites do not correspond to the hydrophobic sites earlier identified in ConA (27,28). There are stacking interactions between the aromatic residues of the peptide and the protein.…”

Section: Discussionmentioning

confidence: 73%

Structural and Functional Consequences of Peptide-Carbohydrate Mimicry

Jain¹,

Kaur

Sundaravadivel

et al. 2000

Journal of Biological Chemistry

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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 ␣-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.

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Section: Discussionmentioning

confidence: 73%

Structural and Functional Consequences of Peptide-Carbohydrate Mimicry

Jain¹,

Kaur

Sundaravadivel

et al. 2000

Journal of Biological Chemistry

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“…The hydrophobic residues that delineate the whole cavity are extremely conserved among ConA and other lectins, and this hydrophobic pocket was involved in the binding of nonpolar molecules, such as iodinated derivatives of aromatic and sugar compounds, and the plant hormone auxin (3-indoleacetic acid) in ConA (51)(52). There has been no report of such binding in arcelin-1, and the x-ray structure suggests that the side chains of the hydrophilic residues (Asn 55 121 and Arg 128 in arcelin-1, respectively.…”

Section: Structure Of Arcelin-1 At 19 å Resolutionmentioning

confidence: 99%

Crystal Structure of the Arcelin-1 Dimer fromPhaseolus vulgarisat 1.9-Å Resolution

Mourey¹,

Pédelacq²,

Birck³

et al. 1998

Journal of Biological Chemistry

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Arcelin-1 is a glycoprotein from kidney beans (Phaseolus vulgaris) which displays insecticidal properties and protects the seeds from predation by larvae of various bruchids. This lectin-like protein is devoid of monosaccharide binding properties and belongs to the phytohemagglutinin protein family. The x-ray structure determination at 1.9-Å resolution of native arcelin-1 dimers, which correspond to the functional state of the protein in solution, was solved using multiple isomorphous replacement and refined to a crystallographic R factor of 0.208. The three glycosylation sites on each monomer are all covalently modified. One of these oligosaccharide chains provides interactions with protein atoms at the dimer interface, and another one may act by preventing the formation of higher oligomeric species in the arcelin variants. The dimeric structure and the severe alteration of the monosaccharide binding site in arcelin-1 correlate with the hemagglutinating properties of the protein, which are unaffected by simple sugars and sugar derivatives. Sequence analysis and structure comparisons of arcelin-1 with the other insecticidal proteins from kidney beans, arcelin-5, and ␣-amylase inhibitor and with legume lectins, yield insights into the molecular basis of the different biological functions of these proteins.

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“…When both metal binding sites are filed, a saccharide binding site is activated. In addition, recent evidence suggests that con A binds a variety of non-polar compounds [2]. Nuclear magnetic resonance and high resolution X-ray crystallographic data have shown that metal ion, saccharide and hydrophobic group binding sites are spatially distinct.…”

Section: Introductionmentioning

confidence: 99%