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Science 15 October 1993:
Vol. 262. no. 5132, pp. 387 - 395
DOI: 10.1126/science.8211159
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Articles

Science, Vol 262, Issue 5132, 387-395
Copyright © 1993 by American Association for the Advancement of Science

articles

Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control

HE Parge, AS Arvai, DJ Murtari, SI Reed, and JA Tainer

The Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.

The cell cycle regulatory protein CksHs2 binds to the catalytic subunit of the cyclin-dependent kinases (Cdk's) and is essential for their biological function. The crystal structure of the protein was determined at 2.1 A resolution. The CksHs2 structure is an unexpected hexamer formed by the symmetric assembly of three interlocked dimers into an unusual 12-stranded beta barrel fold that may represent a prototype for this class of protein structures. Sequence-conserved regions form the unusual beta strand exchange between the subunits of the dimer, and the metal and anion binding sites associated with the hexamer assembly. The two other sequence-conserved regions line a 12 A diameter tunnel through the beta barrel and form the six exposed, charged helix pairs. Six kinase subunits can be modeled to bind the assembled hexamer without collision, and therefore this CksHs2 hexamer may participate in cell cycle control by acting as the hub for Cdk multimerization in vivo.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Folding and Fibril Formation of the Cell Cycle Protein Cks1.
R. Bader, M. A. Seeliger, S. E. Kelly, L. L. Ilag, F. Meersman, A. Limones, B. F. Luisi, C. M. Dobson, and L. S. Itzhaki (2006)
J. Biol. Chem. 281, 18816-18824
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Role of Conformational Heterogeneity in Domain Swapping and Adapter Function of the Cks Proteins.
M. A. Seeliger, M. Spichty, S. E. Kelly, M. Bycroft, S. M. V. Freund, M. Karplus, and L. S. Itzhaki (2005)
J. Biol. Chem. 280, 30448-30459
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Three Different Binding Sites of Cks1 Are Required for p27-Ubiquitin Ligation.
D. Sitry, M. A. Seeliger, T. K. Ko, D. Ganoth, S. E. Breward, L. S. Itzhaki, M. Pagano, and A. Hershko (2002)
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Solution NMR Study of the Monomeric Form of p13suc1 Protein Sheds Light on the Hinge Region Determining the Affinity for a Phosphorylated Substrate.
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Directed Mutagenesis Studies of the Metal Binding Site at the Subunit Interface of Escherichia coli Inorganic Pyrophosphatase.
I. S. Efimova, A. Salminen, P. Pohjanjoki, J. Lapinniemi, N. N. Magretova, B. S. Cooperman, A. Goldman, R. Lahti, and A. A. Baykov (1999)
J. Biol. Chem. 274, 3294-3299
   Abstract »    Full Text »    PDF »
Regulation of Cdc28 Cyclin-Dependent Protein Kinase Activity during the Cell Cycle of the Yeast Saccharomyces cerevisiae.
M. D. Mendenhall and A. E. Hodge (1998)
Microbiol. Mol. Biol. Rev. 62, 1191-1243
   Abstract »    Full Text »    PDF »
The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution.
Y. Liu, P. J. Hart, M. P. Schlunegger, and D. Eisenberg (1998)
PNAS 95, 3437-3442
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Binding of Activated Cyclosome to p13suc1. USE FOR AFFINITY PURIFICATION.
V. Sudakin, M. Shteinberg, D. Ganoth, J. Hershko, and A. Hershko (1997)
J. Biol. Chem. 272, 18051-18059
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Xe-p9, a Xenopus Suc1/Cks homolog, has multiple essential roles in cell cycle control..
D Patra and W G Dunphy (1996)
Genes & Dev. 10, 1503-1515
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p13SUC1 and the WW Domain of PIN1 Bind to the Same Phosphothreonine-Proline Epitope.
I. Landrieu, B. Odaert, J.-M. Wieruszeski, H. Drobecq, P. Rousselot-Pailley, D. Inze, and G. Lippens (2001)
J. Biol. Chem. 276, 1434-1438
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