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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
44
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pubmed:dateCreated |
2006-11-3
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pubmed:abstractText |
We have engineered a variant of the beta-clam shell protein ILBP which lacks the alpha-helical motif that caps the central binding cavity; the mutant protein is sufficiently destabilised that it is unfolded under physiological conditions, however, it unexpectedly binds its natural bile acid substrates with high affinity forming a native-like beta-sheet rich structure and demonstrating strong thermodynamic coupling between ligand binding and protein folding.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1359-7345
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4623-5
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pubmed:meshHeading |
pubmed-meshheading:17082863-Animals,
pubmed-meshheading:17082863-Binding Sites,
pubmed-meshheading:17082863-Cholic Acids,
pubmed-meshheading:17082863-Ligands,
pubmed-meshheading:17082863-Molecular Conformation,
pubmed-meshheading:17082863-Organic Anion Transporters, Sodium-Dependent,
pubmed-meshheading:17082863-Protein Conformation,
pubmed-meshheading:17082863-Protein Engineering,
pubmed-meshheading:17082863-Protein Folding,
pubmed-meshheading:17082863-Protein Structure, Secondary,
pubmed-meshheading:17082863-Rabbits,
pubmed-meshheading:17082863-Stereoisomerism,
pubmed-meshheading:17082863-Structure-Activity Relationship,
pubmed-meshheading:17082863-Symporters,
pubmed-meshheading:17082863-Temperature
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pubmed:year |
2006
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pubmed:articleTitle |
Coupling ligand recognition to protein folding in an engineered variant of rabbit ileal lipid binding protein.
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pubmed:affiliation |
Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, University Park, Nottingham, UKNG7 2RD.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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