ArticleProtein science : a publication of the Protein Society2018
Structural characterization of the catalytic γ and regulatory β subunits of phosphorylase kinase in the context of the hexadecameric enzyme complex.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 8 citations in OpenAlex.
- Molecular basis for the regulation of human phosphorylase kinase by phosphorylation and CaNature communications · 2025Article
- Architecture and activation of human muscle phosphorylase kinase.Nature communications · 2024Article
- A critical evaluation of protein kinase regulation by activation loop autophosphorylation.eLife · 2023Article
- Parameter Reliability and Understanding Enzyme Function.Molecules (Basel, Switzerland) · 2022Review
- An Integrated Approach for Determining a Protein-Protein Binding Interface in Solution and an Evaluation of Hydrogen-Deuterium Exchange Kinetics for Adjudicating Candidate Docking Models.Analytical chemistry · 2019Article
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4 authors at 1 institution in 1 country.
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Abstract
In the tightly regulated glycogenolysis cascade, the breakdown of glycogen to glucose-1-phosphate, phosphorylase kinase (PhK) plays a key role in regulating the activity of glycogen phosphorylase. PhK is a 1.3 MDa hexadecamer, with four copies each of four different subunits (α, β, γ and δ), making the study of its structure challenging. Using hydrogen-deuterium exchange, we have analyzed the regulatory β subunit and the catalytic γ subunit in the context of the intact non-activated PhK complex to study the structure of these subunits and identify regions of surface exposure. Our data suggest that within the non-activated complex the γ subunit assumes an activated conformation and are consistent with a previous docking model of the β subunit within the cryoelectron microscopy envelope of PhK.
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