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rdf:type |
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lifeskim:mentions |
umls-concept:C0010531,
umls-concept:C0024485,
umls-concept:C0037003,
umls-concept:C0379710,
umls-concept:C0441633,
umls-concept:C0599219,
umls-concept:C0600499,
umls-concept:C1514562,
umls-concept:C1522290,
umls-concept:C1704675,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
3
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pubmed:dateCreated |
2006-2-27
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pubmed:abstractText |
The techniques of phage-displayed homolog shotgun scanning, oligomer complementation, NMR secondary structure analysis, and computational docking provide a complementary suite of tools for dissecting protein-protein interactions. Focusing these tools on the interaction between the catalytic sub-unit of protein kinase A (PKAcat) and caveolin-1 scaffolding domain (CSD) reveals the first structural model for the interaction. Homolog shotgun scanning varied each CSD residue as either a wild-type or a homologous amino acid. Wild-type to homolog ratios from 116 different homologous CSD variants identified side-chain functional groups responsible for precise contacts with PKAcat. Structural analysis by NMR assigned an alpha-helical conformation to the central residues 84- 97 of CSD. The extensive mutagenesis data and NMR secondary structure information provided constraints for developing a model for the PKAcat-CSD interaction. Addition of synthetic CSD to phage-displayed CSD resulted in oligomer complementation, or enhanced binding to PKAcat. Together with previous experiments examining the interaction between CSD and endothelial nitric oxide synthase (eNOS), the results suggest a general oligomerization-dependent enhancement of binding between signal transducing enzymes and caveolin-1.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16452625-10473592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16452625-10542274,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16452625-8910575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16452625-9020162,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16452625-9754713
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
478-86
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16452625-Binding Sites,
pubmed-meshheading:16452625-Catalytic Domain,
pubmed-meshheading:16452625-Caveolin 1,
pubmed-meshheading:16452625-Computational Biology,
pubmed-meshheading:16452625-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:16452625-Models, Molecular,
pubmed-meshheading:16452625-Mutation,
pubmed-meshheading:16452625-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:16452625-Peptide Library,
pubmed-meshheading:16452625-Protein Structure, Secondary,
pubmed-meshheading:16452625-Protein Structure, Tertiary,
pubmed-meshheading:16452625-Protein Subunits
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pubmed:year |
2006
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pubmed:articleTitle |
Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking.
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pubmed:affiliation |
Department of Chemistry, University of California, Irvine, CA 92697, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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