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New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria.

Abstract:
The inhibition of enzymes employing a nucleophilic serine residue by natural products has been studied for many years. More recently, high-resolution structural analyses have begun to augment kinetic analyses. In this issue of Chemistry and Biology, Schulz and colleagues describe the crystal structure of scyptolin A, a cyclic peptide produced by cyanobacteria, complexed with elastase. Together with structures for a related inhibitor bound to trypsin, the work may assist in the design of reversible serine protease inhibitors.
Publication status:
Published

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Authors


McDonough, MA More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Journal:
Chemistry and biology
Volume:
10
Issue:
10
Pages:
898-900
Publication date:
2003-10-05
DOI:
EISSN:
1879-1301
ISSN:
1074-5521
URN:
uuid:dad24507-960b-495c-ad66-1dc89ff9a2ff
Source identifiers:
32526
Local pid:
pubs:32526

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