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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 Mul...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2914947458

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

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

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2024-01

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

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

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