New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria.
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 structu...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2003
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| _version_ | 1826299882855464960 |
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| author | McDonough, M Schofield, C |
| author_facet | McDonough, M Schofield, C |
| author_sort | McDonough, M |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T05:08:43Z |
| format | Journal article |
| id | oxford-uuid:dad24507-960b-495c-ad66-1dc89ff9a2ff |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:08:43Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:dad24507-960b-495c-ad66-1dc89ff9a2ff2022-03-27T09:05:57ZNew structural insights into the inhibition of serine proteases by cyclic peptides from bacteria.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:dad24507-960b-495c-ad66-1dc89ff9a2ffEnglishSymplectic Elements at Oxford2003McDonough, MSchofield, CThe 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. |
| spellingShingle | McDonough, M Schofield, C New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria. |
| title | New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria. |
| title_full | New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria. |
| title_fullStr | New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria. |
| title_full_unstemmed | New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria. |
| title_short | New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria. |
| title_sort | new structural insights into the inhibition of serine proteases by cyclic peptides from bacteria |
| work_keys_str_mv | AT mcdonoughm newstructuralinsightsintotheinhibitionofserineproteasesbycyclicpeptidesfrombacteria AT schofieldc newstructuralinsightsintotheinhibitionofserineproteasesbycyclicpeptidesfrombacteria |