Literature DB >> 8411162

Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag.

F Zhang1, D J Robbins, M H Cobb, E J Goldsmith.   

Abstract

The extracellular signal-regulated kinase ERK2, a member of the protein kinase superfamily, phosphorylates a variety of cellular proteins in response to extracellular signals. ERK2 expressed in Escherichia coli as a fusion protein with the sequence Ala-His6 at the N terminus has low basal activity and very low levels of phosphate incorporation, but can be fully activated. The Ala-His6 ERK2 as expressed in the unphosphorylated form has been crystallized in space group P2(1). The cell constants are a = 49.32 A, b = 71.42 A, c = 61.25 A, and beta = 109.75 degrees, and the crystals diffract to better than 1.8 A resolution.

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Year:  1993        PMID: 8411162     DOI: 10.1006/jmbi.1993.1532

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  6 in total

1.  C. elegans GLA-3 is a novel component of the MAP kinase MPK-1 signaling pathway required for germ cell survival.

Authors:  Ekaterini A Kritikou; Stuart Milstein; Pierre-Olivier Vidalain; Guillaume Lettre; Erica Bogan; Kimon Doukoumetzidis; Phillip Gray; Thomas G Chappell; Marc Vidal; Michael O Hengartner
Journal:  Genes Dev       Date:  2006-08-15       Impact factor: 11.361

2.  Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain.

Authors:  Justine M Hill; Hema Vaidyanathan; Joe W Ramos; Mark H Ginsberg; Milton H Werner
Journal:  EMBO J       Date:  2002-12-02       Impact factor: 11.598

3.  Regulation of the activity of MEK kinase 1 (MEKK1) by autophosphorylation within the kinase activation domain.

Authors:  J C Deak; D J Templeton
Journal:  Biochem J       Date:  1997-02-15       Impact factor: 3.857

4.  The Two Non-Visual Arrestins Engage ERK2 Differently.

Authors:  Nicole A Perry-Hauser; Jesse B Hopkins; Ya Zhuo; Chen Zheng; Ivette Perez; Kathryn M Schultz; Sergey A Vishnivetskiy; Ali I Kaya; Pankaj Sharma; Kevin N Dalby; Ka Young Chung; Candice S Klug; Vsevolod V Gurevich; T M Iverson
Journal:  J Mol Biol       Date:  2022-01-22       Impact factor: 5.469

5.  Structural basis of substrate recognition by hematopoietic tyrosine phosphatase.

Authors:  David A Critton; Antoni Tortajada; Geoffrey Stetson; Wolfgang Peti; Rebecca Page
Journal:  Biochemistry       Date:  2008-12-16       Impact factor: 3.162

6.  PEA-15 engages in allosteric interactions using a common scaffold in a phosphorylation-dependent manner.

Authors:  Joyce Ikedife; Jianlin He; Yufeng Wei
Journal:  Sci Rep       Date:  2022-01-07       Impact factor: 4.379

  6 in total

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