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Dynamic allostery-based molecular workings of kinase: peptide complexes

Dynamic allostery-based molecular workings of kinase: peptide complexes

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6660753

Dynamic allostery-based molecular workings of kinase: peptide complexes

About this item

Full title

Dynamic allostery-based molecular workings of kinase: peptide complexes

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2019-07, Vol.116 (30), p.15052-15061

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

A dense interplay between structure and dynamics underlies the working of proteins, especially enzymes. Protein kinases are molecular switches that are optimized for their regulation rather than catalytic turnover rates. Using long-simulations dynamic allostery analysis, this study describes an exploration of the dynamic kinase:peptide complex. We...

Alternative Titles

Full title

Dynamic allostery-based molecular workings of kinase: peptide complexes

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6660753

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6660753

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1900163116

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