Cell-cycle inhibition by independent CDK and PCNA binding domains in p21 super cip1
Article Abstract:
The cyclin-dependent kinases (CDK) and proliferating cell nuclear antigen (PCNA) inhibitory activities of p21 is functionally independent and resides in separate protein domains from p27 and p57. p21, p27 and p57 belongs to a family of proteins that bind to and inhibit CDK required for initiation of S phase. The PCNA and CDK inhibitory and binding activities of p21 respectively resides in the C-terminal domain and N-terminal domain. p21 can inhibit cell-cycle progression by two separate stoichiometric mechanisms and their effectiveness in inhibition is dependent on the relative abundance of CDKs and PCNA.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Article Abstract:
CyclinA's involvement in the activation of the catalytic cyclin-dependent kinase (CDK) can be better understood through the determination of the crystal structure of human cyclinA-cyclin-dependent kinase (CDK)2-ATP complex. The determination reveals that cyclin binding causes conformational changes in the active site of CDK2 that are probably responsible for the activity. The alpha 1 helix of CDK2, which contains the PSTAIRE sequence found in cyclin-dependent kinases, rotates about its axis and the T-loop of CDK2 also moves, removing the blockade to the catalytic site, for phosphorylation to proceed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Mutations increasing autoinhibition inactivate tumour supressors Smad2 and Smad4
Article Abstract:
Tumour-suppressor proteins Smad2 and Smad4 inhibit growth when stimulated by the growth factor TGF-beta. The inhibitory function of the N domain involves interaction the C domain that stops the association of Smad2 with Smad4, and this is particularly increased in tumour-derived forms of Smad 2 and four. Mutations in the C domain upset the effector functions of the Smad proteins. However N-domain arginine mutations inhibit Smad signalling via autoinhibitory functions.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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