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| [[Image:1fqi.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1fqi| PDB=1fqi | SCENE= }} | | {{STRUCTURE_1fqi| PDB=1fqi | SCENE= }} |
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| '''RGS9 RGS DOMAIN'''
| | ===RGS9 RGS DOMAIN=== |
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| ==Overview==
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| A multitude of heptahelical receptors use heterotrimeric G proteins to transduce signals to specific effector target molecules. The G protein transducin, Gt, couples photon-activated rhodopsin with the effector cyclic GMP phosophodiesterase (PDE) in the vertebrate phototransduction cascade. The interactions of the Gt alpha-subunit (alpha(t)) with the inhibitory PDE gamma-subunit (PDEgamma) are central to effector activation, and also enhance visual recovery in cooperation with the GTPase-activating protein regulator of G-protein signalling (RGS)-9 (refs 1-3). Here we describe the crystal structure at 2.0 A of rod transducin alpha x GDP x AlF4- in complex with the effector molecule PDEgamma and the GTPase-activating protein RGS9. In addition, we present the independently solved crystal structures of the RGS9 RGS domain both alone and in complex with alpha(t/i1) x GDP x AlF4-. These structures reveal insights into effector activation, synergistic GTPase acceleration, RGS9 specificity and RGS activity. Effector binding to a nucleotide-dependent site on alpha(t) sequesters PDEgamma residues implicated in PDE inhibition, and potentiates recruitment of RGS9 for hydrolytic transition state stabilization and concomitant signal termination.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11234020}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11234020 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11234020}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rgs9]] | | [[Category: Rgs9]] |
| [[Category: Rod]] | | [[Category: Rod]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:38:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:47:15 2008'' |
