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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1996-10-24
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pubmed:abstractText |
The periplasmic oligopeptide-binding protein OppA has a remarkably broad substrate specificity, binding peptides of two or five amino-acid residues with high affinity, but little regard to sequence. It is therefore an ideal system for studying how different chemical groups can be accommodated in a protein interior. The ability of the protein to bind peptides of different lengths has been studied by co-crystallising it with different ligands.
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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 |
Dec
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1395-406
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8747465-Amino Acid Sequence,
pubmed-meshheading:8747465-Bacterial Proteins,
pubmed-meshheading:8747465-Carrier Proteins,
pubmed-meshheading:8747465-Chemistry, Physical,
pubmed-meshheading:8747465-Crystallography, X-Ray,
pubmed-meshheading:8747465-HLA Antigens,
pubmed-meshheading:8747465-Hydrogen Bonding,
pubmed-meshheading:8747465-Ligands,
pubmed-meshheading:8747465-Lipoproteins,
pubmed-meshheading:8747465-Models, Molecular,
pubmed-meshheading:8747465-Molecular Sequence Data,
pubmed-meshheading:8747465-Oligopeptides,
pubmed-meshheading:8747465-Physicochemical Phenomena,
pubmed-meshheading:8747465-Polylysine,
pubmed-meshheading:8747465-Protein Binding,
pubmed-meshheading:8747465-Protein Structure, Tertiary,
pubmed-meshheading:8747465-Salmonella typhimurium,
pubmed-meshheading:8747465-Uranium
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pubmed:year |
1995
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pubmed:articleTitle |
The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands.
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pubmed:affiliation |
Department of Chemistry, University of York, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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