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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
14
|
| pubmed:dateCreated |
1990-6-13
|
| pubmed:databankReference | |
| pubmed:abstractText |
The cDNA for rat liver glycogen synthase was isolated by screening a rat liver cDNA library constructed in lambda gt11. The cDNA was 2.4 kilobases in length and encoded a protein of 703 amino acid residues with a molecular mass of 80.5 kDa. Comparison of the rat liver and the human muscle sequences show that the amino- and carboxyl-terminal regions are quite divergent as compared to the internal sequences which show an 80% identity. The rat liver carboxyl-terminal region is truncated by 33 residues and has only 46% identity with the muscle sequence but retains the common feature of a low content of hydrophobic amino acids (13%). Phosphorylation sites 1a and 1b, which are the primary targets for phosphorylation by cAMP-dependent protein kinase, are absent in the liver sequence. The presence of these divergent, structurally anomalous carboxyl-terminal regions in liver and muscle glycogen synthase suggests the absence of the requirement that they possess a tertiary structure that is integral to that of the protein core. A model is proposed in which this region interacts with a catalytic core to maintain the I state, and in which phosphorylation serves to uncouple this interaction.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
265
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
7843-8
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2110561-Amino Acid Sequence,
pubmed-meshheading:2110561-Animals,
pubmed-meshheading:2110561-Base Sequence,
pubmed-meshheading:2110561-Binding Sites,
pubmed-meshheading:2110561-Cloning, Molecular,
pubmed-meshheading:2110561-DNA,
pubmed-meshheading:2110561-Deoxyribonuclease EcoRI,
pubmed-meshheading:2110561-Glycogen Synthase,
pubmed-meshheading:2110561-Humans,
pubmed-meshheading:2110561-Liver,
pubmed-meshheading:2110561-Molecular Sequence Data,
pubmed-meshheading:2110561-Molecular Weight,
pubmed-meshheading:2110561-Muscles,
pubmed-meshheading:2110561-Phosphorylation,
pubmed-meshheading:2110561-Protein Biosynthesis,
pubmed-meshheading:2110561-Rabbits,
pubmed-meshheading:2110561-Rats,
pubmed-meshheading:2110561-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:2110561-Sequence Homology, Nucleic Acid
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
The primary structure of rat liver glycogen synthase deduced by cDNA cloning. Absence of phosphorylation sites 1a and 1b.
|
| pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|