TY - JOUR
T1 - The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (β-adrenergic receptor kinase 1)
T2 - A binding partner of G(βγ) subunits
AU - Fushman, David
AU - Najmabadi-Haske, Taraneh
AU - Cahill, Sean
AU - Zheng, Jie
AU - LeVine, Harry
AU - Cowburn, David
PY - 1998/1/30
Y1 - 1998/1/30
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0032579379&partnerID=8YFLogxK
U2 - 10.1074/jbc.273.5.2835
DO - 10.1074/jbc.273.5.2835
M3 - Article
C2 - 9446593
AN - SCOPUS:0032579379
SN - 0021-9258
VL - 273
SP - 2835
EP - 2843
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 5
ER -