Molecular Simulations Reveal an Unresolved Conformation of the Type IA Protein Kinase A Regulatory Subunit and Suggest Its Role in the cAMP Regulatory Mechanism.

Biochemistry. 2017 Aug 01;56(30):3885-3888. doi:10.1021/acs.biochem.7b00461. Epub 2017 Jul 17

{{ author.authorName }}^{{{getOrganisationIndexOf(author)}}} {{ author.authorName }}^{{{getOrganisationIndexOf(author)}}}

+ et al

[No authors listed]

Author information

^{{index+1}} {{ organisation }}

摘要

We identify a previously unresolved, unrecognized, and highly stable conformation of the protein kinase A regulatory subunit RIÎ±. This conformation, which we term the "Flipback" structure, bridges conflicting characteristics in crystallographic structures and solution experiments of the RIÎ± heterotetramer. Our simulations reveal a hinge residue, G235, in the B/C helix that is conserved through all isoforms of RI. Brownian dynamics simulations suggest that the Flipback conformation plays a role in cAMP association to the A domain of the R subunit.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}

基因功能

{{$index+1}}.{{ gene }}

图表

‹ › ×

原始数据

保存测序数据

Sample name	Organism	Experiment title	Sample type	Library instrument	Attributes
Sample name	Organism	Experiment title	Sample type	Library instrument	{{attr}}
{{ dataList.sampleTitle }}	{{ dataList.organism }}	{{ dataList.expermentTitle }}	{{ dataList.sampleType }}	{{ dataList.libraryInstrument }}	{{ showAttributeName(index,attr,dataList.attributes) }}

Molecular Simulations Reveal an Unresolved Conformation of the Type IA Protein Kinase A Regulatory Subunit and Suggest Its Role in the cAMP Regulatory Mechanism.

摘要

基因功能

图表

基因

原始数据

文献解读

分析平台

分析平台

分析流程

{{currentAnalyse.title}}