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 Gβγ SUBUNITS
Title | 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 Gβγ SUBUNITS |
Publication Type | Journal Articles |
Year of Publication | 1998 |
Authors | Fushman D, Najmabadi-Haske T, Cahill S, Zheng J, LeVine H, Cowburn D |
Journal | Journal of Biological ChemistryJ. Biol. Chem. |
Volume | 273 |
Issue | 5 |
Pagination | 2835 - 2843 |
Date Published | 1998/01/30/ |
ISBN Number | 0021-9258, 1083-351X |
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 Gβγ 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. |
URL | http://www.jbc.org/content/273/5/2835 |
DOI | 10.1074/jbc.273.5.2835 |