Substrate and docking interactions in serine/threonine protein kinases

Elizabeth J. Goldsmith, Radha Akella, Xiaoshan Min, Tianjun Zhou, John M. Humphreys

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

The current structural data available on distinct serine/threonine protein kinases have been outlined. It also includes description of how kinases bind substrates at the active site, focusing on the P+1 pocket, which is remodeled in inactive forms of several protein kinases. Other topics tackled include substrate docking interactions outside the active site observed in mitogen-activated protein (MAP) kinases, cyclin dependent kinases (CDKs), and AGC kinases and how specificity among these different families of kinases is achieved from the organization of the binding site.

Original languageEnglish (US)
Pages (from-to)5065-5081
Number of pages17
JournalChemical Reviews
Volume107
Issue number11
DOIs
StatePublished - Nov 2007

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Protein-Serine-Threonine Kinases
Phosphotransferases
Substrates
Cyclin-Dependent Kinases
Mitogen-Activated Protein Kinases
Protein Kinases
Binding Sites

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Substrate and docking interactions in serine/threonine protein kinases. / Goldsmith, Elizabeth J.; Akella, Radha; Min, Xiaoshan; Zhou, Tianjun; Humphreys, John M.

In: Chemical Reviews, Vol. 107, No. 11, 11.2007, p. 5065-5081.

Research output: Contribution to journalArticle

Goldsmith, Elizabeth J. ; Akella, Radha ; Min, Xiaoshan ; Zhou, Tianjun ; Humphreys, John M. / Substrate and docking interactions in serine/threonine protein kinases. In: Chemical Reviews. 2007 ; Vol. 107, No. 11. pp. 5065-5081.
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