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Article

The structure of a monomeric mutant Cks protein reveals multiple functions for a conserved hinge-region proline.

Journal of molecular biology - 19 Aug 2011

Balog Eva Rose M, Saetern Ou Chong, Finch William, Hoeft Cassidy O, Thai Vu, Harvey Stacy L, Kellogg Douglas R, Rubin Seth M

Abstract excerpt

Cks (cyclin-dependent kinase subunit) proteins are essential eukaryotic cell cycle regulatory proteins that physically associate with cyclin-dependent kinases (Cdks) to modulate their activity. Cks proteins have also been studied for their ability to form domain-swapped dimers by exchanging β-strands. Domain swapping is mediated by a conserved β-hinge region containing two proline residues. Previous structural...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 21704044
DOI: 10.1016/j.jmb.2011.05.045

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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