A dynamic hydrophobic core orchestrates allostery in protein kinases-Reference-Cited by-同舟云学术

A dynamic hydrophobic core orchestrates allostery in protein kinases

Published:2017-04-07 Issue:4 Volume:3 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Kim Jonggul¹²,Ahuja Lalima G.³^ORCID,Chao Fa-An²^ORCID,Xia Youlin²^ORCID,McClendon Christopher L.³⁴^ORCID,Kornev Alexandr P.³^ORCID,Taylor Susan S.³⁴,Veglia Gianluigi¹²

Affiliation:

1. Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.

2. Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

3. Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, USA.

4. Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, CA 92093, USA.

Abstract

The synchronized motions of inner core residues allosterically modulate the activity of the protein kinase A catalytic subunit.

Funder

Foundation for the National Institutes of Health

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference54 articles.

1. KinMutBase, a database of human disease-causing protein kinase mutations

2. The Protein Kinase Complement of the Human Genome

3. The Conformational Plasticity of Protein Kinases

4. Dynamics of cAMP-Dependent Protein Kinase

5. A helix scaffold for the assembly of active protein kinases

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