2trc
From Proteopedia
(New page: 200px<br /><applet load="2trc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2trc, resolution 2.4Å" /> '''PHOSDUCIN/TRANSDUCIN ...) |
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| - | [[Image:2trc.gif|left|200px]]<br /><applet load="2trc" size=" | + | [[Image:2trc.gif|left|200px]]<br /><applet load="2trc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2trc, resolution 2.4Å" /> | caption="2trc, resolution 2.4Å" /> | ||
'''PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX'''<br /> | '''PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of transducin's betagamma subunits complexed with | + | The crystal structure of transducin's betagamma subunits complexed with phosducin, which regulates Gtbetagamma activity, has been solved to 2.4 angstroms resolution. Phosducin has two domains that wrap around Gtbetagamma to form an extensive interface. The N-terminal domain binds loops on the "top" Gtbeta surface, overlapping the Gtalpha binding surface, explaining how phosducin blocks Gtbetagamma's interaction with Gtalpha. The C-terminal domain shows structural homology to thioredoxin and binds the outer strands of Gtbeta's seventh and first blades in a manner likely to disrupt Gtbetagamma's normal orientation relative to the membrane and receptor. Phosducin's Ser-73, which when phosphorylated inhibits phosducin's function, points away from Gtbetagamma, toward a large flexible loop. Thus phosphorylation is not likely to affect the interface directly, but rather indirectly through an induced conformational change. |
==About this Structure== | ==About this Structure== | ||
| - | 2TRC 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 Rattus norvegicus] with GD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2TRC 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 Rattus norvegicus] with <scene name='pdbligand=GD:'>GD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TRC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bohm, A.]] | [[Category: Bohm, A.]] | ||
[[Category: Gaudet, R.]] | [[Category: Gaudet, R.]] | ||
| - | [[Category: Sigler, P | + | [[Category: Sigler, P B.]] |
[[Category: GD]] | [[Category: GD]] | ||
[[Category: beta-gamma]] | [[Category: beta-gamma]] | ||
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[[Category: vision]] | [[Category: vision]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:59 2008'' |
Revision as of 16:49, 21 February 2008
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PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX
Overview
The crystal structure of transducin's betagamma subunits complexed with phosducin, which regulates Gtbetagamma activity, has been solved to 2.4 angstroms resolution. Phosducin has two domains that wrap around Gtbetagamma to form an extensive interface. The N-terminal domain binds loops on the "top" Gtbeta surface, overlapping the Gtalpha binding surface, explaining how phosducin blocks Gtbetagamma's interaction with Gtalpha. The C-terminal domain shows structural homology to thioredoxin and binds the outer strands of Gtbeta's seventh and first blades in a manner likely to disrupt Gtbetagamma's normal orientation relative to the membrane and receptor. Phosducin's Ser-73, which when phosphorylated inhibits phosducin's function, points away from Gtbetagamma, toward a large flexible loop. Thus phosphorylation is not likely to affect the interface directly, but rather indirectly through an induced conformational change.
About this Structure
2TRC is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin., Gaudet R, Bohm A, Sigler PB, Cell. 1996 Nov 1;87(3):577-88. PMID:8898209
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