Three protein kinase structures define a common motif (Q40700407)

22 September 2017

title

Three protein kinase structures define a common motif (English)

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22 September 2017

Taylor SS

1

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22 September 2017

Radzio-Andzelm E

series ordinal

2

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22 September 2017

publication date

1 May 1994

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22 September 2017

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22 September 2017

volume

2

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22 September 2017

issue

5

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22 September 2017

page(s)

345-355

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publication type of scholarly work

22 September 2017

review article

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The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

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Structural framework for the protein kinase family

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

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2.0 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent

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Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor

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2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor

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cAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer

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Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations

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Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation

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Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15

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Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide

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The P-loop--a common motif in ATP- and GTP-binding proteins

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Structural basis of the intrasteric regulation of myosin light chain kinases

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A three-dimensional model of the Cdc2 protein kinase: localization of cyclin- and Suc1-binding regions and phosphorylation sites

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Mutations at sites involved in Suc1 binding inactivate Cdc2.

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Energetic limits of phosphotransfer in the catalytic subunit of cAMP-dependent protein kinase as measured by viscosity experiments

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Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation

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A conserved helix motif complements the protein kinase core

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An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase

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7 January 2021

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Identifiers

DOI

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22 September 2017

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