The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (β-adrenergic receptor kinase 1): A binding partner of G(βγ) subunits

David Fushman, Taraneh Najmabadi-Haske, Sean Cahill, Jie Zheng, Harry LeVine, David Cowburn

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

The solution structure of an extended pleckstrin homology (PH) domain from the β-adrenergic receptor kinase is obtained by high resolution NMR. The structure establishes that the β-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 α-helix that behaves as a molten helix, and a surface charge polarity that is extensively modified by positive residues in the extended α-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 G(βγ) 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.

Original languageEnglish (US)
Pages (from-to)2835-2843
Number of pages9
JournalJournal of Biological Chemistry
Volume273
Issue number5
DOIs
StatePublished - Jan 30 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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