1omw: Difference between revisions

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New page: left|200px<br /><applet load="1omw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1omw, resolution 2.50Å" /> '''Crystal Structure of...
 
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[[Image:1omw.gif|left|200px]]<br /><applet load="1omw" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1omw.gif|left|200px]]<br /><applet load="1omw" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1omw, resolution 2.50&Aring;" />
caption="1omw, resolution 2.50&Aring;" />
'''Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits'''<br />
'''Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits'''<br />


==Overview==
==Overview==
The phosphorylation of heptahelical receptors by heterotrimeric guanine, nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is, a universal regulatory mechanism that leads to desensitization of G, protein signaling and to the activation of alternative signaling, pathways.We determined the crystallographic structure of bovine GRK2 in, complex with G protein beta1gamma2 subunits.Our results show how the three, domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective, activities and recruit the enzyme to the cell membrane in an orientation, that not only facilitates receptor phosphorylation, but also allows for, the simultaneous inhibition of signaling by Galpha and Gbetagamma, subunits.
The phosphorylation of heptahelical receptors by heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is a universal regulatory mechanism that leads to desensitization of G protein signaling and to the activation of alternative signaling pathways.We determined the crystallographic structure of bovine GRK2 in complex with G protein beta1gamma2 subunits.Our results show how the three domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective activities and recruit the enzyme to the cell membrane in an orientation that not only facilitates receptor phosphorylation, but also allows for the simultaneous inhibition of signaling by Galpha and Gbetagamma subunits.


==About this Structure==
==About this Structure==
1OMW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [http://en.wikipedia.org/wiki/[Beta-adrenergic-receptor]_kinase [Beta-adrenergic-receptor] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.15 2.7.11.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OMW OCA].  
1OMW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [http://en.wikipedia.org/wiki/[Beta-adrenergic-receptor]_kinase [Beta-adrenergic-receptor] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.15 2.7.11.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMW OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: [Beta-adrenergic-receptor] kinase]]
[[Category: [Beta-adrenergic-receptor] kinase]]
[[Category: Capel, W.D.]]
[[Category: Capel, W D.]]
[[Category: Lefkowitz, R.J.]]
[[Category: Lefkowitz, R J.]]
[[Category: Lodowski, D.T.]]
[[Category: Lodowski, D T.]]
[[Category: Pitcher, J.A.]]
[[Category: Pitcher, J A.]]
[[Category: Tesmer, J.J.G.]]
[[Category: Tesmer, J J.G.]]
[[Category: wd-40 repeat]]
[[Category: wd-40 repeat]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:01:04 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:24 2008''

Revision as of 15:19, 21 February 2008

File:1omw.gif


1omw, resolution 2.50Å

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Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits

OverviewOverview

The phosphorylation of heptahelical receptors by heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is a universal regulatory mechanism that leads to desensitization of G protein signaling and to the activation of alternative signaling pathways.We determined the crystallographic structure of bovine GRK2 in complex with G protein beta1gamma2 subunits.Our results show how the three domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective activities and recruit the enzyme to the cell membrane in an orientation that not only facilitates receptor phosphorylation, but also allows for the simultaneous inhibition of signaling by Galpha and Gbetagamma subunits.

About this StructureAbout this Structure

1OMW is a Protein complex structure of sequences from Bos taurus. Active as [Beta-adrenergic-receptor_kinase [Beta-adrenergic-receptor] kinase], with EC number 2.7.11.15 Full crystallographic information is available from OCA.

ReferenceReference

Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma., Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ, Science. 2003 May 23;300(5623):1256-62. PMID:12764189 [[Category: [Beta-adrenergic-receptor] kinase]]

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