1bak
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(New page: 200px<br /> <applet load="1bak" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bak" /> '''SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOM...)
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Revision as of 14:01, 12 November 2007
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SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPLED RECEPTOR KINASE 2 (BETA-ADRENERGIC RECEPTOR KINASE 1), C-TERMINAL EXTENDED, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1BAK is a Single protein structure of sequence from Homo sapiens. Active as [Beta-adrenergic-receptor_kinase [Beta-adrenergic-receptor] kinase], with EC number 2.7.11.15 Full crystallographic information is available from OCA.
Reference
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., Fushman D, Najmabadi-Haske T, Cahill S, Zheng J, LeVine H 3rd, Cowburn D, J Biol Chem. 1998 Jan 30;273(5):2835-43. PMID:9446593[[Category: [Beta-adrenergic-receptor] kinase]]
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