2b9r
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Crystal Structure of Human Cyclin B1
OverviewOverview
Cyclin B is the key regulatory protein controlling mitosis in all, eukaryotes, where it binds cyclin-dependent kinase, cdk1, forming a, complex which initiates the mitotic program through phosphorylation of, select proteins. Cyclin B regulates the activation, subcellular, localization, and substrate specificity of cdk1, and destruction of cyclin, B is necessary for mitotic exit. Overexpression of human cyclin B1 has, been found in numerous cancers and has been associated with tumor, aggressiveness. Here we report the crystal structure of human cyclin B1 to, 2.9 A. Comparison of the structure with cyclin A and cyclin E reveals, remarkably similar N-terminal cyclin box motifs but significant, differences among the C-terminal cyclin box lobes. Divergence in sequence, gives rise to unique interaction surfaces at the proposed cyclin B/cdk1, interface as well as the 'RxL' motif substrate binding site on cyclin B., Examination of the structure provides insight into the molecular basis for, differential affinities of protein based cyclin/cdk inhibitors such as, p27, substrate recognition, and cdk interaction.
About this StructureAbout this Structure
2B9R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of human cyclin B., Petri ET, Errico A, Escobedo L, Hunt T, Basavappa R, Cell Cycle. 2007 Jun;6(11):1342-9. Epub 2007 Jun 14. PMID:17495533
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