Source:http://linkedlifedata.com/resource/pubmed/id/17510962
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2007-7-26
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pubmed:abstractText |
Inhibitor-1alpha is one of the isoforms of human protein phosphatase inhibitor-1. It is a product of alternative splicing of inhibitor-1 gene and lacks 51 internal amino acids from residue 84 to 134 of inhibitor-1. Here we have characterized the structural and biochemical properties of inhibitor-1alpha. Structural analysis of recombinant inhibitor-1alpha by NMR spectroscopy revealed that inhibitor-1alpha adopts a predominantly random coil conformation. Excluding the region from residue 84 to 134 of inhibitor-1, the structural features of inhibitor-1 and inhibitor-1alpha are almost the same as each other. The IC(50) value of inhibitor-1alpha in inhibition of Protein phosphatase-1 (PP1) is comparable to that of inhibitor-1, indicating that inhibitor-1alpha is a potent inhibitor of PP1 when Thr-35 is phosphorylated by PKA. For phosphorylation by PKA and dephosphorylation by protein phosphatase-1, -2A, and -2B, the measured kinetic parameters of inhibitor-1alpha are very close to those of inhibitor-1. Taken together, these results suggest that inhibitor-1alpha preserves the structure of inhibitor-1, the PP1 inhibitory activity and the functional specificities toward phosphorylation by PKA and dephosphorylation by protein phosphatase-1, -2A, and -2B.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ANP32A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1097-0134
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
68
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
779-88
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17510962-Animals,
pubmed-meshheading:17510962-Catalytic Domain,
pubmed-meshheading:17510962-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:17510962-DNA, Complementary,
pubmed-meshheading:17510962-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:17510962-Kinetics,
pubmed-meshheading:17510962-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17510962-Phosphoprotein Phosphatases,
pubmed-meshheading:17510962-Phosphorylation,
pubmed-meshheading:17510962-Protein Conformation,
pubmed-meshheading:17510962-Protein Phosphatase 1,
pubmed-meshheading:17510962-Rabbits,
pubmed-meshheading:17510962-Recombinant Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Structural and biochemical characterization of inhibitor-1alpha.
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pubmed:affiliation |
Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 621, Taiwan, Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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