ATP-Binding Free Energy Simulations Reveal an Allosteric Link Between the Enzyme Active Site and Mul...
ATP-Binding Free Energy Simulations Reveal an Allosteric Link Between the Enzyme Active Site and Multiple Functional Protein-Protein Interaction Interfaces in Cyclin Dependent Kinase-1
About this item
Full title
Author / Creator
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Journal title
Language
English
Formats
Publication information
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Subjects
More information
Scope and Contents
Contents
The ATP dependent phosphorylation activity of Cyclin Dependent Kinase 1 (CDK1), an essential enzyme for cell cycle progression, is intrinsically dependent upon interactions with Cyclin-B, substrate, and Cks proteins. A recent joint experimental-computational study from our group showed intriguingly that acetylation at the active site abrogated the...
Alternative Titles
Full title
ATP-Binding Free Energy Simulations Reveal an Allosteric Link Between the Enzyme Active Site and Multiple Functional Protein-Protein Interaction Interfaces in Cyclin Dependent Kinase-1
Authors, Artists and Contributors
Author / Creator
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_journals_2914947458
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2914947458
Other Identifiers
E-ISSN
2692-8205
DOI
10.1101/2024.01.15.575662
How to access this item
https://www.proquest.com/docview/2914947458?pq-origsite=primo&accountid=13902