Regulation of protein kinases; controlling activity through activation segment conformation.

Molecular cell ·Vol. 15 ·No. 5 ·2004-09-10 ·Pages 661-75

Nolen B, Taylor S, Ghosh G

Abstract

There are currently at least forty-six unique protein kinase crystal structures, twenty-four of which are available in an active state. Here we examine these structures using a structural bioinformatics approach to understand how the conformation of the activation segment controls kinase activity.

MeSH Terms

Amino Acid Motifs/physiology Animals Catalytic Domain/physiology Computational Biology Humans Models, Molecular Molecular Conformation Phosphorylation Protein Kinases/chemistry Protein Structure, Tertiary/physiology Sequence Homology, Amino Acid Structure-Activity Relationship

Chemicals

Protein Kinases

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Nolen Brad

Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92116, USA.

Taylor Susan

Ghosh Gourisankar

Article Info

Journal

Molecular cell

Abbr.

Mol Cell

ISSN

1097-2765

DOI

10.1016/j.molcel.2004.08.024

Published

2004-09-10

Pages

661-75

Language

English

Region

United States

NLM ID

9802571

Subset

External Links

PubMed source DOI: 10.1016/j.molcel.2004.08.024 View journal details

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Regulation of protein kinases; controlling activity through activation segment conformation.

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