Crystallization of MAP kinases

Seung Jae Lee, Tianjun Zhou, Elizabeth J. Goldsmith

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

X-ray structural studies of MAP kinases and MAP kinase module components are elucidating how kinase activity is regulated and how specificity of signaling is conferred. In the past decade, MAP kinases have been crystallized in their active, phosphorylated forms or low-activity, unphosphorylated forms, as well as in the presence of binding partners such as docking peptides and inhibitors. Crystallization has been achieved via diverse strategies including control of phosphorylation, coding sequence modification, incorporation of tags for purification, and use of a variety of cell-types for protein expression. Recently, interest has been focused on use of crystallography for lead optimization in the development for pharmacological inhibitors on MAP kinases. Further, some success has been gained in crystallizing the MAP kinase activators MAP2Ks and MAP3K kinase domains. This review describes the key methods that have been utilized to crystallize MAP kinases and MAP kinase pathway components.

Original languageEnglish (US)
Pages (from-to)224-233
Number of pages10
JournalMethods
Volume40
Issue number3
DOIs
StatePublished - Nov 2006

Fingerprint

Crystallization
Phosphotransferases
Mitogen-Activated Protein Kinase Kinases
Crystallography
Phosphorylation
MAP Kinase Signaling System
Purification
X-Rays
Pharmacology
X rays
Peptides
Proteins

Keywords

  • Crystallization
  • Docking peptide
  • MAP kinases
  • Phosphorylation
  • Tethering

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Crystallization of MAP kinases. / Lee, Seung Jae; Zhou, Tianjun; Goldsmith, Elizabeth J.

In: Methods, Vol. 40, No. 3, 11.2006, p. 224-233.

Research output: Contribution to journalArticle

Lee, Seung Jae ; Zhou, Tianjun ; Goldsmith, Elizabeth J. / Crystallization of MAP kinases. In: Methods. 2006 ; Vol. 40, No. 3. pp. 224-233.
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