We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ym7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ym7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ym7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ym7| PDB=1ym7 | SCENE= }}
{{STRUCTURE_1ym7| PDB=1ym7 | SCENE= }}
-
'''G Protein-Coupled Receptor Kinase 2 (GRK2)'''
+
===G Protein-Coupled Receptor Kinase 2 (GRK2)===
-
==Overview==
+
<!--
-
In response to extracellular signals, G protein-coupled receptors (GPCRs) catalyze guanine nucleotide exchange on Galpha subunits, enabling both activated Galpha and Gbetagamma subunits to target downstream effector enzymes. One target of Gbetagamma is G protein-coupled receptor kinase 2 (GRK2), an enzyme that initiates homologous desensitization by phosphorylating activated GPCRs. GRK2 consists of three distinct domains: an RGS homology (RH) domain, a protein kinase domain, and a pleckstrin homology (PH) domain, through which it binds Gbetagamma. The crystal structure of the GRK2-Gbetagamma complex revealed that the domains of GRK2 are intimately associated and left open the possibility for allosteric regulation by Gbetagamma. In this paper, we report the 4.5 A structure of GRK2, which shows that the binding of Gbetagamma does not induce large domain rearrangements in GRK2, although small rotations of the RH and PH domains relative to the kinase domain are evident. Mutation of residues within the larger domain interfaces of GRK2 generally leads to diminished expression and activity, suggesting that these interfaces are important for stability and remain intact upon activation of GRK2. Geranylgeranylated Gbetagamma, but not a soluble mutant of Gbetagamma, protects GRK2 from clostripain digestion at a site within its kinase domain that is 80 A away from the Gbetagamma binding site. Equilibrium ultracentrifugation experiments indicate that neither abnormally large detergent micelles nor protein oligomerization can account for the observed protection. The Gbetagamma-mediated binding of GRK2 to CHAPS micelles or lipid bilayers therefore appears to rigidify the kinase domain, perhaps by encouraging stable contacts between the RH and kinase domains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15865441}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15865441 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15865441}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Grk2]]
[[Category: Grk2]]
[[Category: Kinase]]
[[Category: Kinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:30:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:09:25 2008''

Revision as of 14:09, 28 July 2008

Image:1ym7.png

Template:STRUCTURE 1ym7

G Protein-Coupled Receptor Kinase 2 (GRK2)

Template:ABSTRACT PUBMED 15865441

About this Structure

1YM7 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

The role of G beta gamma and domain interfaces in the activation of G protein-coupled receptor kinase 2., Lodowski DT, Barnhill JF, Pyskadlo RM, Ghirlando R, Sterne-Marr R, Tesmer JJ, Biochemistry. 2005 May 10;44(18):6958-70. PMID:15865441

Page seeded by OCA on Mon Jul 28 17:09:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ym7"
Personal tools