Matches in SemOpenAlex for { <https://semopenalex.org/work/W2084231535> ?p ?o ?g. }
Showing items 1 to 53 of
53
with 100 items per page.
- W2084231535 endingPage "c176" @default.
- W2084231535 startingPage "c176" @default.
- W2084231535 abstract "CDK7, a member of the cyclin-dependent protein kinase family, regulates the activities of other CDKs through phosphorylation on their activation segment and hence contributes to control of the eukaryotic cell cycle. CDK7 also assists in the regulation of transcription as part of the transcription factor TFIIH complex. For maximum activity and stability, CDK7 requires phosphorylation, association with cyclin H, and association with a third protein, MAT1. We have determined the crystal structure of human CDK7 in complex with ATP at 3 A resolution. The kinase is in the inactive conformation, similar to that observed for inactive CDK2. The activation segment is phosphorylated at Thr170 and is in a defined conformation that differs from that in phospho-CDK2 and phospho-CDK2/cyclin A. The functional properties of the enzyme against CDK2 and CTD as substrates are characterized through kinase assays. Experiments confirm that CDK7 is not a substrate for kinase-associated phosphatase." @default.
- W2084231535 created "2016-06-24" @default.
- W2084231535 creator A5021059453 @default.
- W2084231535 creator A5021285723 @default.
- W2084231535 creator A5042362798 @default.
- W2084231535 creator A5044928766 @default.
- W2084231535 date "2005-08-23" @default.
- W2084231535 modified "2023-09-25" @default.
- W2084231535 title "The crystal structure of human CDK7 and its protein recognition properties" @default.
- W2084231535 doi "https://doi.org/10.1107/s0108767305092494" @default.
- W2084231535 hasPublicationYear "2005" @default.
- W2084231535 type Work @default.
- W2084231535 sameAs 2084231535 @default.
- W2084231535 citedByCount "0" @default.
- W2084231535 crossrefType "journal-article" @default.
- W2084231535 hasAuthorship W2084231535A5021059453 @default.
- W2084231535 hasAuthorship W2084231535A5021285723 @default.
- W2084231535 hasAuthorship W2084231535A5042362798 @default.
- W2084231535 hasAuthorship W2084231535A5044928766 @default.
- W2084231535 hasBestOaLocation W20842315351 @default.
- W2084231535 hasConcept C115624301 @default.
- W2084231535 hasConcept C185592680 @default.
- W2084231535 hasConcept C192562407 @default.
- W2084231535 hasConcept C70721500 @default.
- W2084231535 hasConcept C8010536 @default.
- W2084231535 hasConcept C86803240 @default.
- W2084231535 hasConceptScore W2084231535C115624301 @default.
- W2084231535 hasConceptScore W2084231535C185592680 @default.
- W2084231535 hasConceptScore W2084231535C192562407 @default.
- W2084231535 hasConceptScore W2084231535C70721500 @default.
- W2084231535 hasConceptScore W2084231535C8010536 @default.
- W2084231535 hasConceptScore W2084231535C86803240 @default.
- W2084231535 hasIssue "a1" @default.
- W2084231535 hasLocation W20842315351 @default.
- W2084231535 hasOpenAccess W2084231535 @default.
- W2084231535 hasPrimaryLocation W20842315351 @default.
- W2084231535 hasRelatedWork W1969215021 @default.
- W2084231535 hasRelatedWork W1969352129 @default.
- W2084231535 hasRelatedWork W2011272194 @default.
- W2084231535 hasRelatedWork W2012932458 @default.
- W2084231535 hasRelatedWork W2063698282 @default.
- W2084231535 hasRelatedWork W2082823139 @default.
- W2084231535 hasRelatedWork W2315457165 @default.
- W2084231535 hasRelatedWork W2711806730 @default.
- W2084231535 hasRelatedWork W2890061065 @default.
- W2084231535 hasRelatedWork W2950083354 @default.
- W2084231535 hasVolume "61" @default.
- W2084231535 isParatext "false" @default.
- W2084231535 isRetracted "false" @default.
- W2084231535 magId "2084231535" @default.
- W2084231535 workType "article" @default.