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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1998-2-23
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pubmed:databankReference |
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pubmed:abstractText |
The solution structure of an extended pleckstrin homology (PH) domain from the beta-adrenergic receptor kinase is obtained by high resolution NMR. The structure establishes that the beta-adrenergic receptor kinase extended PH domain has the same fold and topology as other PH domains, and there are several unique features, most notably an extended C-terminal alpha-helix that behaves as a molten helix, and a surface charge polarity that is extensively modified by positive residues in the extended alpha-helix and the C terminus. These observations complement biochemical evidence that the C-terminal portion of this PH domain participates in protein-protein interactions with Gbetagamma subunits. This suggests that the C-terminal segment of the PH domain may function to mediate protein-protein interactions with the targets of PH domains.
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pubmed:grant |
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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 |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2835-43
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9446593-Amino Acid Sequence,
pubmed-meshheading:9446593-Binding Sites,
pubmed-meshheading:9446593-Blood Proteins,
pubmed-meshheading:9446593-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:9446593-Dimerization,
pubmed-meshheading:9446593-GTP-Binding Proteins,
pubmed-meshheading:9446593-Humans,
pubmed-meshheading:9446593-Models, Molecular,
pubmed-meshheading:9446593-Molecular Sequence Data,
pubmed-meshheading:9446593-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9446593-Peptide Fragments,
pubmed-meshheading:9446593-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:9446593-Phosphoproteins,
pubmed-meshheading:9446593-Protein Binding,
pubmed-meshheading:9446593-Protein Structure, Secondary,
pubmed-meshheading:9446593-Recombinant Proteins,
pubmed-meshheading:9446593-Sequence Homology, Amino Acid,
pubmed-meshheading:9446593-Static Electricity,
pubmed-meshheading:9446593-beta-Adrenergic Receptor Kinases
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pubmed:year |
1998
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pubmed:articleTitle |
The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits.
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pubmed:affiliation |
Laboratory of Physical Biochemistry, The Rockefeller University, New York, New York 10021-6399, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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