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- W2096039018 abstract "The cyclin D1–cyclin-dependent kinase 4 (CDK4) complex is a key regulator of the transition through the G 1 phase of the cell cycle. Among the cyclin/CDKs, CDK4 and cyclin D1 are the most frequently activated by somatic genetic alterations in multiple tumor types. Thus, aberrant regulation of the CDK4/cyclin D1 pathway plays an essential role in oncogenesis; hence, CDK4 is a genetically validated therapeutic target. Although X-ray crystallographic structures have been determined for various CDK/cyclin complexes, CDK4/cyclin D1 has remained highly refractory to structure determination. Here, we report the crystal structure of CDK4 in complex with cyclin D1 at a resolution of 2.3 Å. Although CDK4 is bound to cyclin D1 and has a phosphorylated T-loop, CDK4 is in an inactive conformation and the conformation of the heterodimer diverges from the previously known CDK/cyclin binary complexes, which suggests a unique mechanism for the process of CDK4 regulation and activation." @default.
- W2096039018 created "2016-06-24" @default.
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- W2096039018 date "2009-03-17" @default.
- W2096039018 modified "2023-10-18" @default.
- W2096039018 title "Crystal structure of human CDK4 in complex with a D-type cyclin" @default.
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- W2096039018 doi "https://doi.org/10.1073/pnas.0809645106" @default.
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