1bak: Difference between revisions

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[[Image:1bak.jpg|left|200px]]
{{Seed}}
[[Image:1bak.png|left|200px]]


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{{STRUCTURE_1bak|  PDB=1bak  |  SCENE=  }}  
{{STRUCTURE_1bak|  PDB=1bak  |  SCENE=  }}  


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




==Overview==
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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 line below this paragraph, {{ABSTRACT_PUBMED_9446593}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9446593 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9446593}}


==About this Structure==
==About this Structure==
1BAK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAK OCA].  
1BAK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAK OCA].  


==Reference==
==Reference==
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[[Category: Pleckstrin homology domain]]
[[Category: Pleckstrin homology domain]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:16:50 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:42:37 2008''

Revision as of 15:42, 30 June 2008

File:1bak.png

Template:STRUCTURE 1bak

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

Template:ABSTRACT PUBMED 9446593

About this Structure

1BAK is a Single protein structure of sequence from Homo sapiens. Full experimental 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

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