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rdf:type |
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lifeskim:mentions |
umls-concept:C0007382,
umls-concept:C0036720,
umls-concept:C0069437,
umls-concept:C0180860,
umls-concept:C0332298,
umls-concept:C0441712,
umls-concept:C0581406,
umls-concept:C1522664,
umls-concept:C1546637,
umls-concept:C1550638,
umls-concept:C1704449,
umls-concept:C1704684
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pubmed:issue |
3
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pubmed:dateCreated |
2001-3-20
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pubmed:databankReference |
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pubmed:abstractText |
Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-10329620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-10504726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-10607670,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-10716187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-10747969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-1569074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-1812006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-1840588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-1900195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-1953688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-2026166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-3292288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-3330562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-6358755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-7492323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-7501240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-7845207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-8038298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-8387132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-8691432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-9434107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11256612-9695945
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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 |
Sep
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pubmed:issn |
1469-221X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
277-81
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11256612-Amino Acid Substitution,
pubmed-meshheading:11256612-Animals,
pubmed-meshheading:11256612-Brain,
pubmed-meshheading:11256612-Catalysis,
pubmed-meshheading:11256612-Crystallography, X-Ray,
pubmed-meshheading:11256612-Cysteine,
pubmed-meshheading:11256612-Disulfides,
pubmed-meshheading:11256612-Enzyme Stability,
pubmed-meshheading:11256612-Glutathione Disulfide,
pubmed-meshheading:11256612-Hydrogen-Ion Concentration,
pubmed-meshheading:11256612-Kinetics,
pubmed-meshheading:11256612-Models, Molecular,
pubmed-meshheading:11256612-Mutation,
pubmed-meshheading:11256612-Oxidation-Reduction,
pubmed-meshheading:11256612-Protein Conformation,
pubmed-meshheading:11256612-Recombinant Proteins,
pubmed-meshheading:11256612-Serine Endopeptidases,
pubmed-meshheading:11256612-Substrate Specificity,
pubmed-meshheading:11256612-Swine,
pubmed-meshheading:11256612-Temperature
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pubmed:year |
2000
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pubmed:articleTitle |
Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
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pubmed:affiliation |
Department of Biological Sciences, University of Warwick, Coventry, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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