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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1995-1-19
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pubmed:abstractText |
Glycopeptide antibiotics of the vancomycin group are of crucial clinical importance in the treatment of methicillin resistant Staphylococcus aureus (MRSA)--the often lethal 'super-bug'--characterized by its resistance to a wide range of antibiotics in common use. The antibiotics exert their physiological action by blocking cell wall synthesis through recognition of nascent cell wall mucopeptides terminating in the sequence -D-Ala-D-Ala. Evidence suggests that the antibiotics are able to enhance their biological activity by the formation of homodimers, and this is supported by the observation that dimerization and peptide binding in vitro are cooperative phenomena. The basis of this enhancement is not understood at the molecular level.
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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 |
Aug
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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 |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
747-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7994574-Amino Acid Sequence,
pubmed-meshheading:7994574-Anti-Bacterial Agents,
pubmed-meshheading:7994574-Binding Sites,
pubmed-meshheading:7994574-Cell Wall,
pubmed-meshheading:7994574-Computer Simulation,
pubmed-meshheading:7994574-Disaccharides,
pubmed-meshheading:7994574-Glycopeptides,
pubmed-meshheading:7994574-Hydrogen Bonding,
pubmed-meshheading:7994574-Magnetic Resonance Spectroscopy,
pubmed-meshheading:7994574-Models, Molecular,
pubmed-meshheading:7994574-Molecular Sequence Data,
pubmed-meshheading:7994574-Oligopeptides,
pubmed-meshheading:7994574-Protein Binding,
pubmed-meshheading:7994574-Protein Conformation,
pubmed-meshheading:7994574-Vancomycin
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pubmed:year |
1994
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pubmed:articleTitle |
The structure of an asymmetric dimer relevant to the mode of action of the glycopeptide antibiotics.
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pubmed:affiliation |
Cambridge Centre for Molecular Recognition, University Chemical Laboratories, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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