ParkinsonCanadaV1, Main, Exploration, bibRecord, 001299

A 22-mer Segment in the Structurally Pliable Regulatory Domain of Metazoan CTP: Phosphocholine Cytidylyltransferase Facilitates Both Silencing and Activating Functions*

Identifieur interne : 001299 ( Main/Exploration ); précédent : 001298; suivant : 001300

A 22-mer Segment in the Structurally Pliable Regulatory Domain of Metazoan CTP: Phosphocholine Cytidylyltransferase Facilitates Both Silencing and Activating Functions*

Auteurs : Ziwei Ding ; Svetla G. Taneva ; Harris K. H. Huang ; Stephanie A. Campbell ; Lucie Semenec ; Nansheng Chen ; Rosemary B. Cornell [Canada]

Source :

The Journal of Biological Chemistry [ 0021-9258 ] ; 2012.

RBID : PMC:3493939

English descriptors

KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Animals, Catalysis, Catalytic Domain, Choline-Phosphate Cytidylyltransferase (chemistry), Choline-Phosphate Cytidylyltransferase (physiology), Computational Biology (methods), Cytidine Triphosphate (chemistry), Enzyme Activation, Gene Silencing, Kinetics, Lipids (chemistry), Molecular Sequence Data, Phosphatidylcholines (chemistry), Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Rats, Sequence Homology, Amino Acid, alpha-Synuclein (chemistry).
MESH :
- chemical , chemistry : Choline-Phosphate Cytidylyltransferase, Cytidine Triphosphate, Lipids, Phosphatidylcholines, alpha-Synuclein.
- chemical , physiology : Choline-Phosphate Cytidylyltransferase.
- methods : Computational Biology.
- Amino Acid Motifs, Amino Acid Sequence, Animals, Catalysis, Catalytic Domain, Enzyme Activation, Gene Silencing, Kinetics, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Rats, Sequence Homology, Amino Acid.

Abstract

Background: The mechanism whereby CCT is auto-inhibited by its membrane-induced amphipathic helix (m-AH) is unknown.

Results: m-AH regions sharing an amphipathic 22-mer element can be interchanged between CCTs with retention of catalytic silencing and activation by lipids.

Conclusion: The 22-mer element is the principal auto-inhibitory motif.

Significance: Multi-tasking and conformationally malleable motifs are widely used to regulate protein function; the CCT m-AH is a novel example of this.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3493939

DOI: 10.1074/jbc.M112.402081
PubMed: 22988242
PubMed Central: 3493939

Affiliations:

Canada

Le document en format XML

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<term>Choline-Phosphate Cytidylyltransferase (chemistry)</term>
<term>Choline-Phosphate Cytidylyltransferase (physiology)</term>
<term>Computational Biology (methods)</term>
<term>Cytidine Triphosphate (chemistry)</term>
<term>Enzyme Activation</term>
<term>Gene Silencing</term>
<term>Kinetics</term>
<term>Lipids (chemistry)</term>
<term>Molecular Sequence Data</term>
<term>Phosphatidylcholines (chemistry)</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
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<term>Rats</term>
<term>Sequence Homology, Amino Acid</term>
<term>alpha-Synuclein (chemistry)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Choline-Phosphate Cytidylyltransferase</term>
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<term>Phosphatidylcholines</term>
<term>alpha-Synuclein</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Choline-Phosphate Cytidylyltransferase</term>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
 The mechanism whereby CCT is auto-inhibited by its membrane-induced amphipathic helix (m-AH) is unknown.</p>
<p><bold>Results:</bold>
 m-AH regions sharing an amphipathic 22-mer element can be interchanged between CCTs with retention of catalytic silencing and activation by lipids.</p>
<p><bold>Conclusion:</bold>
 The 22-mer element is the principal auto-inhibitory motif.</p>
<p><bold>Significance:</bold>
 Multi-tasking and conformationally malleable motifs are widely used to regulate protein function; the CCT m-AH is a novel example of this.</p>
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La maladie de Parkinson au Canada (serveur d'exploration)

A 22-mer Segment in the Structurally Pliable Regulatory Domain of Metazoan CTP: Phosphocholine Cytidylyltransferase Facilitates Both Silencing and Activating Functions*

A 22-mer Segment in the Structurally Pliable Regulatory Domain of Metazoan CTP: Phosphocholine Cytidylyltransferase Facilitates Both Silencing and Activating Functions*

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

	La maladie de Parkinson au Canada (serveur d'exploration)
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