Allosteric Regulation of Proteases
Allostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibi...
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| Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2008-12, Vol.9 (18), p.2920-2928 |
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| container_end_page | 2928 |
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| container_issue | 18 |
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| container_title | Chembiochem : a European journal of chemical biology |
| container_volume | 9 |
| creator | Hauske, Patrick Ottmann, Christian Meltzer, Michael Ehrmann, Michael Kaiser, Markus |
| description | Allostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. The structural bases of some proteinaceous and small-molecule allosteric protease regulators have already been elucidated, indicating a general mechanism that might be exploitable for future rational design of small-molecule effectors. |
| doi_str_mv | 10.1002/cbic.200800528 |
| format | Article |
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Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. 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Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. The structural bases of some proteinaceous and small-molecule allosteric protease regulators have already been elucidated, indicating a general mechanism that might be exploitable for future rational design of small-molecule effectors.</description><subject>Allosteric Regulation</subject><subject>Caspase Inhibitors</subject><subject>Caspases - chemistry</subject><subject>Caspases - metabolism</subject><subject>Chemistry, Pharmaceutical</subject><subject>Crystallography, X-Ray</subject><subject>Drug Design</subject><subject>drug discovery</subject><subject>enzymes</subject><subject>Models, Molecular</subject><subject>Peptide Hydrolases - chemical synthesis</subject><subject>Peptide Hydrolases - chemistry</subject><subject>Peptide Hydrolases - metabolism</subject><subject>proteases</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - metabolism</subject><subject>small molecules</subject><subject>Structure-Activity Relationship</subject><issn>1439-4227</issn><issn>1439-7633</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkDtPwzAURi0EoqWwMkLFwJbiazt2PNIISlF5lgqJxXISpwqkTbETQf89qRIVNqZ7h3O-4SB0DHgAGJOLOMriAcE4wNgnwQ7qAqPSE5zS3fZnhIgOOnDuHWMsOYV91AGJCQCDLjq7zPPClcZmcf_ZzKtcl1mx7Bdp_9EWpdHOuEO0l-rcmaP29tDs-uolvPEmD6NxeDnxYiYg8Bg1WqbAicE0MX4S0EQYSUiktUhoTHjEMBPMTwShNI4iHojAiBQC0AC6lnrovNld2eKzMq5Ui8zFJs_10hSVU1xK4CCDGhw0YGwL56xJ1cpmC23XCrDaVFGbKmpbpRZO2uUqWpjkF28z1IBsgK8sN-t_5lQ4HId_x73GzeqM31tX2w_FBRW-er0fqafRHRvesql6q_nThk91ofTcZk7NpgQDxeALxolPfwDvY4TW</recordid><startdate>20081215</startdate><enddate>20081215</enddate><creator>Hauske, Patrick</creator><creator>Ottmann, Christian</creator><creator>Meltzer, Michael</creator><creator>Ehrmann, Michael</creator><creator>Kaiser, Markus</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20081215</creationdate><title>Allosteric Regulation of Proteases</title><author>Hauske, Patrick ; 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| fulltext | fulltext |
| identifier | ISSN: 1439-4227 |
| ispartof | Chembiochem : a European journal of chemical biology, 2008-12, Vol.9 (18), p.2920-2928 |
| issn | 1439-4227 1439-7633 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Allosteric Regulation Caspase Inhibitors Caspases - chemistry Caspases - metabolism Chemistry, Pharmaceutical Crystallography, X-Ray Drug Design drug discovery enzymes Models, Molecular Peptide Hydrolases - chemical synthesis Peptide Hydrolases - chemistry Peptide Hydrolases - metabolism proteases Protein Conformation Protein Structure, Tertiary Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism small molecules Structure-Activity Relationship |
| title | Allosteric Regulation of Proteases |
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