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PDBsum entry 1jw5
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Sugar binding protein
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PDB id
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1jw5
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands.
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Authors
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X.Duan,
F.A.Quiocho.
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Ref.
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Biochemistry, 2002,
41,
706-712.
[DOI no: ]
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PubMed id
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Abstract
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The receptor, a maltose/maltooligosaccharide-binding protein, has been found to
be an excellent system for the study of molecular recognition because its polar
and nonpolar binding functions are segregated into two globular domains. The
X-ray structures of the "closed" and "open" forms of the protein complexed with
maltose and maltotetraitol have been determined. These sugars have approximately
3 times more accessible polar surface (from OH groups) than nonpolar surface
(from small clusters of sugar ring CH bonds). In the closed structures, the
oligosaccharides are buried in the groove between the two domains of the protein
and bound by extensive hydrogen bonding interactions of the OH groups with the
polar residues confined mostly in one domain and by nonpolar interactions of the
CH clusters with four aromatic residues lodged in the other domain. Substantial
contacts between the sugar hydroxyls and aromatic residues are also formed. In
the open structures, the oligosaccharides are bound almost exclusively in the
domain rich in aromatic residues. This finding, along with the analysis of
buried surface area due to complex formations in the open and closed structures,
supports a major role for nonpolar interactions in initial ligand binding even
when the ligands have significantly greater potential for highly specific polar
interactions.
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