Literature DB >> 7716171

Crystallization and preliminary crystallographic study of human CksHs1: a cell cycle regulatory protein.

A S Arvai1, Y Bourne, D Williams, S I Reed, J A Tainer.   

Abstract

The cell cycle regulatory protein CksHs1 has been crystallized in a form suitable for X-ray studies. CksHs1 crystals were grown in the presence of vanadate, a phosphatase inhibitor, but were also obtained with phosphate or tungstate as a cofactor. They belong to the hexagonal space group P6(1)22 with unit cell dimensions: a = b = 94 A, c = 131.6 A, and gamma = 120 degrees. The crystals grown in the presence of vanadate diffract X-rays to at least 2.8 A. Molecular replacement results from the homologous human CksHs2 structure reveal that a dimer forms the crystal habit, giving the unusual Vm value of 4.4 A3/Da or a solvent content of 72%.

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Year:  1995        PMID: 7716171     DOI: 10.1002/prot.340210109

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  4 in total

1.  Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligase.

Authors:  Kui Xu; Charles Belunis; Wei Chu; David Weber; Frank Podlaski; Kuo-Sen Huang; Steven I Reed; Lyubomir T Vassilev
Journal:  Biochem J       Date:  2003-05-01       Impact factor: 3.857

2.  The Prozone Effect Accounts for the Paradoxical Function of the Cdk-Binding Protein Suc1/Cks.

Authors:  Sang Hoon Ha; Sun Young Kim; James E Ferrell
Journal:  Cell Rep       Date:  2016-02-04       Impact factor: 9.423

3.  Cyclin-stimulated binding of Cks proteins to cyclin-dependent kinases.

Authors:  E A Egan; M J Solomon
Journal:  Mol Cell Biol       Date:  1998-07       Impact factor: 4.272

4.  Cks1: Structure, Emerging Roles and Implications in Multiple Cancers.

Authors:  Vinayak Khattar; Jaideep V Thottassery
Journal:  J Cancer Ther       Date:  2013-10-01
  4 in total

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