2bcj

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(New page: 200px<br /><applet load="2bcj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bcj, resolution 3.061&Aring;" /> '''Crystal Structure o...)
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[[Image:2bcj.gif|left|200px]]<br /><applet load="2bcj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bcj, resolution 3.061&Aring;" />
caption="2bcj, resolution 3.061&Aring;" />
'''Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits'''<br />
'''Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits'''<br />
==Overview==
==Overview==
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G protein-coupled receptor kinase 2 (GRK2) plays a key role in the, desensitization of G protein-coupled receptor signaling by phosphorylating, activated heptahelical receptors and by sequestering heterotrimeric G, proteins. We report the atomic structure of GRK2 in complex with Galphaq, and Gbetagamma, in which the activated Galpha subunit of Gq is fully, dissociated from Gbetagamma and dramatically reoriented from its position, in the inactive Galphabetagamma heterotrimer. Galphaq forms an, effector-like interaction with the GRK2 regulator of G protein signaling, (RGS) homology domain that is distinct from and does not overlap with that, used to bind RGS proteins such as RGS4.
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G protein-coupled receptor kinase 2 (GRK2) plays a key role in the desensitization of G protein-coupled receptor signaling by phosphorylating activated heptahelical receptors and by sequestering heterotrimeric G proteins. We report the atomic structure of GRK2 in complex with Galphaq and Gbetagamma, in which the activated Galpha subunit of Gq is fully dissociated from Gbetagamma and dramatically reoriented from its position in the inactive Galphabetagamma heterotrimer. Galphaq forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4.
==About this Structure==
==About this Structure==
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2BCJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus,mus_musculus Rattus norvegicus,mus musculus] with MG, ALF, ACE and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2BCJ OCA].
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2BCJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus,mus_musculus Rattus norvegicus,mus musculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ALF:'>ALF</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2BCJ OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus,mus musculus]]
[[Category: Rattus norvegicus,mus musculus]]
[[Category: [Beta-adrenergic-receptor] kinase]]
[[Category: [Beta-adrenergic-receptor] kinase]]
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[[Category: Tesmer, J.J.G.]]
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[[Category: Tesmer, J J.G.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: ALF]]
[[Category: ALF]]
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[[Category: wd40 protein]]
[[Category: wd40 protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:43:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:21 2008''

Revision as of 14:36, 21 February 2008


2bcj, resolution 3.061Å

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Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits

Overview

G protein-coupled receptor kinase 2 (GRK2) plays a key role in the desensitization of G protein-coupled receptor signaling by phosphorylating activated heptahelical receptors and by sequestering heterotrimeric G proteins. We report the atomic structure of GRK2 in complex with Galphaq and Gbetagamma, in which the activated Galpha subunit of Gq is fully dissociated from Gbetagamma and dramatically reoriented from its position in the inactive Galphabetagamma heterotrimer. Galphaq forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4.

About this Structure

2BCJ is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus,mus musculus with , , and as ligands. 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

Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex., Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJ, Science. 2005 Dec 9;310(5754):1686-90. PMID:16339447[[Category: [Beta-adrenergic-receptor] kinase]]

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