1BAK

SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPLED RECEPTOR KINASE 2 (BETA-ADRENERGIC RECEPTOR KINASE 1), C-TERMINAL EXTENDED, NMR, 20 STRUCTURES

Summary for 1BAK

• Entry DOI: 10.2210/pdb1bak/pdb
• Descriptor: G-PROTEIN COUPLED RECEPTOR KINASE 2 (1 entity in total)
• Functional Keywords: pleckstrin homology domain, ph domain, signal transduction, g-beta-gamma binding domain, beta-adrenergic receptor kinase, beta-ark, g-protein coupled receptor kinase (grk-2), transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 14214.49

Authors

Fushman, D.,Cowburn, D. (deposition date: 1997-11-21, release date: 1998-02-25, Last modification date: 2024-05-22)

Primary citation

Fushman, D.,Najmabadi-Haske, T.,Cahill, S.,Zheng, J.,LeVine 3rd., H.,Cowburn, D.
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.
J.Biol.Chem., 273:2835-2843, 1998

PubMed Abstract: 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.

PubMed: 9446593
DOI: 10.1074/jbc.273.5.2835

Experimental method

SOLUTION NMR