Activating MAP KAP kinase 2.

Structure (London, England : 1993) ·Vol. 11 ·No. 6 ·2003-06-00 ·Pages 611-2

ter Haar E

Abstract

The crystal structures of MAP KAP kinase 2 in complex with ADP and staurosporine suggest a major reorganization of the glycine-rich loop upon ligand binding. The main determinant for the catalytic activity of MAP KAP kinase 2 is phosphorylation by p38 MAP kinase.

MeSH Terms

Adenosine Diphosphate/metabolism Animals Enzyme Activation Intracellular Signaling Peptides and Proteins Mitogen-Activated Protein Kinases/metabolism Protein Serine-Threonine Kinases/chemistry,metabolism Protein Structure, Tertiary Staurosporine/metabolism p38 Mitogen-Activated Protein Kinases

Chemicals

Intracellular Signaling Peptides and Proteins Adenosine Diphosphate MAP-kinase-activated kinase 2 Protein Serine-Threonine Kinases Mitogen-Activated Protein Kinases p38 Mitogen-Activated Protein Kinases Staurosporine

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

ter Haar Ernst

Article Info

Journal

Structure (London, England : 1993)

Abbr.

Structure

ISSN

0969-2126

DOI

10.1016/s0969-2126(03)00104-7

Published

2003-06-00

Pages

611-2

Language

English

Region

United States

NLM ID

101087697

Subset

Corrections

CommentOn

PMID: 12791252

External Links

PubMed source DOI: 10.1016/s0969-2126(03)00104-7 View journal details

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Activating MAP KAP kinase 2.

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