1973
DOI: 10.1021/bi00746a022
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Binding of nonpolar molecules by crystalline concanavalin A

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Cited by 86 publications
(35 citation statements)
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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%
“…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%
“…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%
“…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%