@article {18723,
	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},
	journal = {Journal of Biological ChemistryJ. Biol. Chem.},
	volume = {273},
	year = {1998},
	month = {1998/01/30/},
	pages = {2835 - 2843},
	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.},
	isbn = {0021-9258, 1083-351X},
	doi = {10.1074/jbc.273.5.2835},
	url = {http://www.jbc.org/content/273/5/2835},
	author = {Fushman, David and Najmabadi-Haske,Taraneh and Cahill,Sean and Zheng,Jie and LeVine,Harry and Cowburn,David}
}
