Acti, cofilin and cognition

Article Abstract:

LIM-kinase 1 (LIMK-1) phosphorylates cofilin, a vital protein that is needed for turnover of actin filaments. Furthermore, LIMK-1, but not an inactive form of the enzyme, can phosphorylate recombinant cofilin. These findings explain why overexpression of LIMK-1 produces an accumulation of excess actin filaments, while overexpression of a dominant-negative LIMK-1 restricts the accumulation of actin filaments. It is possible that a fall in LIMK-1 could explain the abnormally clustered and aligned neurons seen in the brains of patients with Williams syndrome.

Physiological aspects, Actin, Protein deficiency

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Under arrest at atomic resolution

Article Abstract:

Crystal structure of cyclin dependent kinase (Cdk2), complexed with cyclinA and inhibitory subunit p27, reveals that p27 introduces extensive conformational changes in Cdk2 to inhibit its kinase activity. A short amino acid motif on p27 is inserted in the binding pocket on cyclinA. The Beta-turn segment in the carboxy-terminal region of p27 distorts the beta-sheet of the kinase, and the beta-strand segment of p27 displaces the carboxy-terminal segment of p27.

Proteins, Protein structure, Enzyme regulation, Enzyme inhibitors

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Crystal structure of cyclin-dependent kinase 2

Article Abstract:

Cyclin-dependent kinase 2 (CDK2) has a bi-lobate structure with a unique helix-loop segment adjacent to the enzyme's active site that interferes with ATP and protein substrate binding. It is part of a family of protein kinases regulating the eukaryotic cell cycle; activation of the CDKs at cell cycle stages seems to trigger the cell cycle's principal transitions. This study determines CDK2's crystal structure to 2.4 Angstroms.

Models, Protein kinases, Crystals, Crystal structure

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