1bak: Difference between revisions

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==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.

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==

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[[Category: signal transduction]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 24: / Line 24: @@
 [[Category: signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:31:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:24 2008''