Protein Kinase Inhibition By Staurosporine Revealed In Details Of The Molecular Interaction With CDK2

Below is result for Protein Kinase Inhibition By Staurosporine Revealed In Details Of The Molecular Interaction With CDK2 in PDF format. You can download or read online all document for free, but please respect copyrighted ebooks. This site does not host PDF files, all document are the property of their respective owners.

Crystal structure of the tyrosine kinase domain of the

Staurosporine is a potent, nonselective protein kinase inhib-itor, the first of 50 alkaloids with an indolocarbazole subunit isolated to date (15). Structures of staurosporine in complex with the Ser Thr kinase domains of CDK2 and protein kinase A (PKA), as well as the tyrosine kinase domains of CSK and Lck, have been reported (16 19).

Professor Dame Louise Napier Johnson 1940-2012

Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2. Nat. Struct. Biol. 4, 796 801. Lolli, G., Lowe, E.D., Brown, N.R., and Johnson, L.N. (2004). The crystal structure of human CDK7 and its protein recognition properties. Structure 12, 2067 2079. Lowe, E.D., Noble, M.E.M., Skamnaki, V.T.,

Structures of staurosporine bound to CDK2 and cAPK new

Staurosporine bound to CDK2 In the report from the group of Louise Johnson [8], the crystal structure of staurosporine in a binary complex with CDK2, a cell-cycle kinase, provides complementary evi-dence for the binding mode of this inhibitor and provides additional information on the origins of selectivity of related compounds.

Crystal Structure of the Tyrosine Kinase Domain of the

Staurosporine is a potent, nonselective protein kinase inhib-itor, the first of >50 alkaloids with an indolocarbazole subunit isolated to date (15). Structures of staurosporine in complex with the Ser/Thr kinase domains of CDK2 and protein kinase A (PKA), as well as the tyrosine kinase