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PDBsum entry 1fqj
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protein ligands metals Protein-protein interface(s) links
Signaling protein PDB id
1fqj

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
317 a.a. *
133 a.a. *
38 a.a. *
141 a.a. *
Ligands
ALF-GDP ×2
Metals
_MG ×2
Waters ×356
* Residue conservation analysis
PDB id:
1fqj
Name: Signaling protein
Title: Crystal structure of the heterotrimeric complex of the rgs domain of rgs9, the gamma subunit of phosphodiesterase and the gt/i1 chimera alpha subunit [(rgs9)-(pdegamma)-(gt/i1alpha)-(gdp)-(alf4-)-(mg2+)]
Structure: Guanine nucleotide-binding protein g(t) subunit alpha-1, guanine nucleotide-binding protein g(i) subunit alpha-1,guanine nucleotide-binding protein g(t) subunit alpha-1. Chain: a, d. Fragment: unp p04695 residues 26-215 and 295-350 linked via unp p10824 residues 220-298. Synonym: transducin alpha-1 chain,adenylate cyclase-inhibiting g alpha protein,transducin alpha-1 chain. Engineered: yes.
Source: Bos taurus, rattus norvegicus. Bovine, rat. Organism_taxid: 9913, 10116. Gene: gnat1, gnai1, gnai-1. Expressed in: escherichia coli. Expression_system_taxid: 562. Bos taurus. Bovine. Organism_taxid: 9913.
Biol. unit: Pentamer (from PQS)
Resolution:
2.02Å     R-factor:   0.233     R-free:   0.265
Authors: K.C.Slep,M.A.Kercher,W.He,C.W.Cowan,T.G.Wensel,P.B.Sigler
Key ref:
K.C.Slep et al. (2001). Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A. Nature, 409, 1071-1077. PubMed id: 11234020 DOI: 10.1038/35059138
Date:
05-Sep-00     Release date:   28-Feb-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04695  (GNAT1_BOVIN) -  Guanine nucleotide-binding protein G(t) subunit alpha-1 from Bos taurus
Seq:
Struc: 		350 a.a.
317 a.a.*
Protein chains
Pfam   ArchSchema ?
P10824  (GNAI1_RAT) -  Guanine nucleotide-binding protein G(i) subunit alpha-1 from Rattus norvegicus
Seq:
Struc: 		354 a.a.
317 a.a.*
Protein chain
Pfam   ArchSchema ?
O46469  (RGS9_BOVIN) -  Regulator of G-protein signaling 9 from Bos taurus
Seq:
Struc: 		484 a.a.
133 a.a.
Protein chain
Pfam   ArchSchema ?
P04972  (CNRG_BOVIN) -  Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma from Bos taurus
Seq:
Struc: 		87 a.a.
38 a.a.
Protein chain
Pfam   ArchSchema ?
O46469  (RGS9_BOVIN) -  Regulator of G-protein signaling 9 from Bos taurus
Seq:
Struc: 		484 a.a.
141 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 97 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: Chains A, B, D, E: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: Chain C: E.C.3.1.4.35  - 3',5'-cyclic-GMP phosphodiesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 3',5'-cyclic GMP + H2O = GMP + H+
3',5'-cyclic GMP
 + H2O
 =
GMP
Bound ligand (Het Group name = GDP)
matches with 85.71% similarity 		+ H(+)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1038/35059138 Nature 409:1071-1077 (2001)
PubMed id: 11234020  
 
 
Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A.
K.C.Slep, M.A.Kercher, W.He, C.W.Cowan, T.G.Wensel, P.B.Sigler.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
Figure 3.
Figure 3: PDE bold gamma-/ alpha-[t/i1] interactions. a, A-weighted 2F[o] - F[c] electron density map for [t/i1] GDP AlF^-[4] PDE RGS9 (1.5 ). Anomalous difference Fourier density (15 ) in coral. b, Intermolecular contact (sub 4 Å) matrix for PDE residues (orange) that contact [t/i1] non-switch residues (green) or [t/i1] switch residues (blue). Electrostatic interactions to side chains are shown in red, to main chain in green. van der Waals contacts to side chains, to main chain or to both are shown in black, grey and lavender, respectively. Water-mediated interactions are indicated by blue circles. The root-mean-square deviation (rmsd) for [t/i1] contact residues (C atoms are in black, overall side-chain deviation in grey) is shown for [t/i1] RGS9 versus [t] GTP S (left)6 and [t] GDP AlF^-[4] (right)8. Results of PDE alanine scanning mutagenesis on GTPase stimulation (light-green bars) and K[A] (dark-blue bars; ref. 13) are shown above. c, C trace of PDE [50 -87]. C atoms of residues contacting [t/i1] switch II, the 3/ 3 - 5 loop region or both are in blue, green and orange, respectively. d, CPK representation of PDE W70 in the switch II/ 3 groove with residues that contact W70 in orange. e, Diagram of PDE /switch II/RGS9 interactions coloured as in a. f, CPK representation of the heterotrimeric complex with the five C-terminal amino acids of PDE in red. 		Figure 5.
Figure 5: Interaction modes of the G alpha-switch II region with G alpha-effector molecules and the G beta-bold gamma-subunit. a, Interaction of PDE with [t/i1] GDP AlF^-[4]. The colouring scheme is the same as in Fig. 1. b, Interaction of adenylyl cyclase constructs VC[1] (red) and IIC[2] (yellow) with [s] GTP S19. The [s] colouring scheme is homologous to that used for [t/i1] in a. c, Interaction of [259]beta [t] (grey-green) with [260]alpha [t/i1] [261][glyph.gif] GDP (coloured as in a)23.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2001, 409, 1071-1077) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21822282 A.M.Lyon, V.M.Tesmer, V.D.Dhamsania, D.M.Thal, J.Gutierrez, S.Chowdhury, K.C.Suddala, J.K.Northup, and J.J.Tesmer (2011).
An autoinhibitory helix in the C-terminal region of phospholipase C-β mediates Gαq activation.
  Nat Struct Mol Biol, 18, 999.
PDB codes: 3qr0 3qr1
21685921 M.Kosloff, A.M.Travis, D.E.Bosch, D.P.Siderovski, and V.Y.Arshavsky (2011).
Integrating energy calculations with functional assays to decipher the specificity of G protein-RGS protein interactions.
  Nat Struct Mol Biol, 18, 846-853.  
20151179 A.Yamazaki, V.A.Bondarenko, I.Matsuura, M.Tatsumi, S.Kurono, N.Komori, H.Matsumoto, F.Hayashi, R.K.Yamazaki, and J.Usukura (2010).
Mechanism for the regulation of mammalian cGMP phosphodiesterase6. 1: identification of its inhibitory subunit complexes and their roles.
  Mol Cell Biochem, 339, 215-233.  
20457940 A.Zurita, Y.Zhang, L.Pedersen, T.Darden, and L.Birnbaumer (2010).
Obligatory role in GTP hydrolysis for the amide carbonyl oxygen of the Mg(2+)-coordinating Thr of regulatory GTPases.
  Proc Natl Acad Sci U S A, 107, 9596-9601.  
20976244 B.R.Temple, C.D.Jones, and A.M.Jones (2010).
Evolution of a signaling nexus constrained by protein interfaces and conformational States.
  PLoS Comput Biol, 6, e1000962.  
20966218 G.L.Waldo, T.K.Ricks, S.N.Hicks, M.L.Cheever, T.Kawano, K.Tsuboi, X.Wang, C.Montell, T.Kozasa, J.Sondek, and T.K.Harden (2010).
Kinetic scaffolding mediated by a phospholipase C-beta and Gq signaling complex.
  Science, 330, 974-980.
PDB code: 3ohm
20002516 J.N.Talbot, D.L.Roman, M.J.Clark, R.A.Roof, J.J.Tesmer, R.R.Neubig, and J.R.Traynor (2010).
Differential modulation of mu-opioid receptor signaling to adenylyl cyclase by regulators of G protein signaling proteins 4 or 8 and 7 in permeabilised C6 cells is Galpha subtype dependent.
  J Neurochem, 112, 1026-1034.  
20655036 L.Dvir, G.Srour, R.Abu-Ras, B.Miller, S.A.Shalev, and T.Ben-Yosef (2010).
Autosomal-recessive early-onset retinitis pigmentosa caused by a mutation in PDE6G, the gene encoding the gamma subunit of rod cGMP phosphodiesterase.
  Am J Hum Genet, 87, 258-264.  
20001089 L.Shen, G.Caruso, P.Bisegna, D.Andreucci, V.V.Gurevich, H.E.Hamm, and E.Dibenedetto (2010).
Dynamics of mouse rod phototransduction and its sensitivity to variation of key parameters.
  IET Syst Biol, 4, 12.  
19880753 M.Aittaleb, C.A.Boguth, and J.J.Tesmer (2010).
Structure and function of heterotrimeric G protein-regulated Rho guanine nucleotide exchange factors.
  Mol Pharmacol, 77, 111-125.  
19798052 B.Barren, L.Gakhar, H.Muradov, K.K.Boyd, S.Ramaswamy, and N.O.Artemyev (2009).
Structural basis of phosphodiesterase 6 inhibition by the C-terminal region of the gamma-subunit.
  EMBO J, 28, 3613-3622.
PDB codes: 3jwq 3jwr
18827025 B.Jastrzebska, M.Golczak, D.Fotiadis, A.Engel, and K.Palczewski (2009).
Isolation and functional characterization of a stable complex between photoactivated rhodopsin and the G protein, transducin.
  FASEB J, 23, 371-381.  
19760664 H.E.Hamm, S.M.Meier, G.Liao, and A.M.Preininger (2009).
Trp fluorescence reveals an activation-dependent cation-pi interaction in the Switch II region of Galphai proteins.
  Protein Sci, 18, 2326-2335.  
19437048 K.Khafizov (2009).
GoLoco motif proteins binding to Galpha(i1): insights from molecular simulations.
  J Mol Model, 15, 1491-1499.  
18800065 L.L.Blazer, and R.R.Neubig (2009).
Small molecule protein-protein interaction inhibitors as CNS therapeutic agents: current progress and future hurdles.
  Neuropsychopharmacology, 34, 126-141.  
19074425 N.Suzuki, K.Tsumoto, N.Hajicek, K.Daigo, R.Tokita, S.Minami, T.Kodama, T.Hamakubo, and T.Kozasa (2009).
Activation of Leukemia-associated RhoGEF by G{alpha}13 with Significant Conformational Rearrangements in the Interface.
  J Biol Chem, 284, 5000-5009.  
19424291 R.Gasper, S.Meyer, K.Gotthardt, M.Sirajuddin, and A.Wittinghofer (2009).
It takes two to tango: regulation of G proteins by dimerization.
  Nat Rev Mol Cell Biol, 10, 423-429.  
18975915 A.Goc, T.E.Angel, B.Jastrzebska, B.Wang, P.L.Wintrode, and K.Palczewski (2008).
Different properties of the native and reconstituted heterotrimeric G protein transducin.
  Biochemistry, 47, 12409-12419.  
18936096 A.Shankaranarayanan, D.M.Thal, V.M.Tesmer, D.L.Roman, R.R.Neubig, T.Kozasa, and J.J.Tesmer (2008).
Assembly of High Order G{alpha}q-Effector Complexes with RGS Proteins.
  J Biol Chem, 283, 34923-34934.  
18537558 C.A.Johnston, F.S.Willard, J.K.Ramer, R.Blaesius, C.N.Roques, and D.P.Siderovski (2008).
State-selective binding peptides for heterotrimeric G-protein subunits: novel tools for investigating G-protein signaling dynamics.
  Comb Chem High Throughput Screen, 11, 370-381.  
18519563 C.A.Johnston, K.Afshar, J.T.Snyder, G.G.Tall, P.Gönczy, D.P.Siderovski, and F.S.Willard (2008).
Structural determinants underlying the temperature-sensitive nature of a Galpha mutant in asymmetric cell division of Caenorhabditis elegans.
  J Biol Chem, 283, 21550-21558.
PDB codes: 2ebc 3umr
18230733 J.Song, L.W.Guo, H.Muradov, N.O.Artemyev, A.E.Ruoho, and J.L.Markley (2008).
Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure.
  Proc Natl Acad Sci U S A, 105, 1505-1510.
PDB code: 2ju4
18434540 K.C.Slep, M.A.Kercher, T.Wieland, C.K.Chen, M.I.Simon, and P.B.Sigler (2008).
Molecular architecture of Galphao and the structural basis for RGS16-mediated deactivation.
  Proc Natl Acad Sci U S A, 105, 6243-6248.
PDB codes: 3c7k 3c7l
18454845 K.Sayar, O.UÄŸur, T.Liu, V.J.Hilser, and O.Onaran (2008).
Exploring allosteric coupling in the alpha-subunit of Heterotrimeric G proteins using evolutionary and ensemble-based approaches.
  BMC Struct Biol, 8, 23.  
18204463 M.L.Cheever, J.T.Snyder, S.Gershburg, D.P.Siderovski, T.K.Harden, and J.Sondek (2008).
Crystal structure of the multifunctional Gbeta5-RGS9 complex.
  Nat Struct Mol Biol, 15, 155-162.
PDB code: 2pbi
18434541 M.Soundararajan, F.S.Willard, A.J.Kimple, A.P.Turnbull, L.J.Ball, G.A.Schoch, C.Gileadi, O.Y.Fedorov, E.F.Dowler, V.A.Higman, S.Q.Hutsell, M.Sundström, D.A.Doyle, and D.P.Siderovski (2008).
Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits.
  Proc Natl Acad Sci U S A, 105, 6457-6462.
PDB codes: 1zv4 2a72 2af0 2bt2 2bv1 2es0 2gtp 2i59 2ihb 2ihd 2ik8 2jm5 2jnu 2ode 2owi
18329041 R.J.Austin, W.W.Ja, and R.W.Roberts (2008).
Evolution of class-specific peptides targeting a hot spot of the Galphas subunit.
  J Mol Biol, 377, 1406-1418.  
18456304 T.G.Wensel (2008).
Signal transducing membrane complexes of photoreceptor outer segments.
  Vision Res, 48, 2052-2061.  
18043707 W.M.Oldham, and H.E.Hamm (2008).
Heterotrimeric G protein activation by G-protein-coupled receptors.
  Nat Rev Mol Cell Biol, 9, 60-71.  
18940608 Z.Chen, W.D.Singer, S.M.Danesh, P.C.Sternweis, and S.R.Sprang (2008).
Recognition of the activated states of Galpha13 by the rgRGS domain of PDZRhoGEF.
  Structure, 16, 1532-1543.
PDB codes: 3cx6 3cx7 3cx8
17173929 G.X.Xie, and P.P.Palmer (2007).
How regulators of G protein signaling achieve selective regulation.
  J Mol Biol, 366, 349-365.  
17255942 H.Liu, A.Suresh, F.S.Willard, D.P.Siderovski, S.Lu, and N.I.Naqvi (2007).
Rgs1 regulates multiple Galpha subunits in Magnaporthe pathogenesis, asexual growth and thigmotropism.
  EMBO J, 26, 690-700.  
17044014 S.H.Tsang, M.L.Woodruff, L.Jun, V.Mahajan, C.K.Yamashita, R.Pedersen, C.S.Lin, S.P.Goff, T.Rosenberg, M.Larsen, D.B.Farber, and S.Nusinowitz (2007).
Transgenic mice carrying the H258N mutation in the gene encoding the beta-subunit of phosphodiesterase-6 (PDE6B) provide a model for human congenital stationary night blindness.
  Hum Mutat, 28, 243-254.  
17463080 W.M.Oldham, N.Van Eps, A.M.Preininger, W.L.Hubbell, and H.E.Hamm (2007).
Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins.
  Proc Natl Acad Sci U S A, 104, 7927-7932.  
16388592 B.Kreutz, D.M.Yau, M.R.Nance, S.Tanabe, J.J.Tesmer, and T.Kozasa (2006).
A new approach to producing functional G alpha subunits yields the activated and deactivated structures of G alpha(12/13) proteins.
  Biochemistry, 45, 167-174.
PDB codes: 1zca 1zcb
16981699 C.A.Johnston, E.S.Lobanova, A.S.Shavkunov, J.Low, J.K.Ramer, R.Blaesius, Z.Fredericks, F.S.Willard, B.Kuhlman, V.Y.Arshavsky, and D.P.Siderovski (2006).
Minimal determinants for binding activated G alpha from the structure of a G alpha(i1)-peptide dimer.
  Biochemistry, 45, 11390-11400.
PDB code: 2g83
16687250 G.B.Willars (2006).
Mammalian RGS proteins: multifunctional regulators of cellular signalling.
  Semin Cell Dev Biol, 17, 363-376.  
16407279 J.E.Grant, L.W.Guo, M.M.Vestling, K.A.Martemyanov, V.Y.Arshavsky, and A.E.Ruoho (2006).
The N terminus of GTP gamma S-activated transducin alpha-subunit interacts with the C terminus of the cGMP phosphodiesterase gamma-subunit.
  J Biol Chem, 281, 6194-6202.  
17053066 N.Van Eps, W.M.Oldham, H.E.Hamm, and W.L.Hubbell (2006).
Structural and dynamical changes in an alpha-subunit of a heterotrimeric G protein along the activation pathway.
  Proc Natl Acad Sci U S A, 103, 16194-16199.  
16855591 X.Pan, S.Eathiraj, M.Munson, and D.G.Lambright (2006).
TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.
  Nature, 442, 303-306.
PDB code: 2g77
16004878 C.A.Johnston, F.S.Willard, M.R.Jezyk, Z.Fredericks, E.T.Bodor, M.B.Jones, R.Blaesius, V.J.Watts, T.K.Harden, J.Sondek, J.K.Ramer, and D.P.Siderovski (2005).
Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange.
  Structure, 13, 1069-1080.
PDB code: 1y3a
15632124 J.Garzón, M.Rodríguez-Muñoz, A.López-Fando, and P.Sánchez-Blázquez (2005).
Activation of mu-opioid receptors transfers control of Galpha subunits to the regulator of G-protein signaling RGS9-2: role in receptor desensitization.
  J Biol Chem, 280, 8951-8960.  
16041481 N.G.Abdulaev, C.Zhang, A.Dinh, T.Ngo, P.N.Bryan, D.M.Brabazon, J.P.Marino, and K.D.Ridge (2005).
Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein alpha-subunit.
  J Biomol NMR, 32, 31-40.  
16045448 S.Jo, K.H.Lee, S.Song, Y.K.Jung, and C.S.Park (2005).
Identification and functional characterization of cereblon as a binding protein for large-conductance calcium-activated potassium channel in rat brain.
  J Neurochem, 94, 1212-1224.  
16339447 V.M.Tesmer, T.Kawano, A.Shankaranarayanan, T.Kozasa, and J.J.Tesmer (2005).
Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex.
  Science, 310, 1686-1690.
PDB code: 2bcj
15665872 Z.Chen, W.D.Singer, P.C.Sternweis, and S.R.Sprang (2005).
Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator.
  Nat Struct Mol Biol, 12, 191-197.
PDB code: 1shz
15485848 B.Y.Lee, C.D.Thulin, and B.M.Willardson (2004).
Site-specific phosphorylation of phosducin in intact retina. Dynamics of phosphorylation and effects on G protein beta gamma dimer binding.
  J Biol Chem, 279, 54008-54017.  
15128951 C.J.Thomas, X.Du, P.Li, Y.Wang, E.M.Ross, and S.R.Sprang (2004).
Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein alpha-subunit.
  Proc Natl Acad Sci U S A, 101, 7560-7565.
PDB codes: 1svk 1svs
15485891 J.Vázquez-Prado, H.Miyazaki, M.D.Castellone, H.Teramoto, and J.S.Gutkind (2004).
Chimeric G alpha i2/G alpha 13 proteins reveal the structural requirements for the binding and activation of the RGS-like (RGL)-containing Rho guanine nucleotide exchange factors (GEFs) by G alpha 13.
  J Biol Chem, 279, 54283-54290.  
15368366 M.V.Hinrichs, M.Montecino, M.Bunster, and J.Olate (2004).
Mutation of the highly conserved Arg165 and Glu168 residues of human Gsalpha disrupts the alphaD-alphaE loop and enhances basal GDP/GTP exchange rate.
  J Cell Biochem, 93, 409-417.  
14724630 P.F.Egea, S.O.Shan, J.Napetschnig, D.F.Savage, P.Walter, and R.M.Stroud (2004).
Substrate twinning activates the signal recognition particle and its receptor.
  Nature, 427, 215-221.
PDB code: 1rj9
15471870 P.W.Day, J.J.Tesmer, R.Sterne-Marr, L.C.Freeman, J.L.Benovic, and P.B.Wedegaertner (2004).
Characterization of the GRK2 binding site of Galphaq.
  J Biol Chem, 279, 53643-53652.  
15123672 Q.Zhang, A.Dickson, and C.A.Doupnik (2004).
Gbetagamma-activated inwardly rectifying K(+) (GIRK) channel activation kinetics via Galphai and Galphao-coupled receptors are determined by Galpha-specific interdomain interactions that affect GDP release rates.
  J Biol Chem, 279, 29787-29796.  
15271992 S.Majumdar, S.Ramachandran, and R.A.Cerione (2004).
Perturbing the linker regions of the alpha-subunit of transducin: a new class of constitutively active GTP-binding proteins.
  J Biol Chem, 279, 40137-40145.  
12560335 G.Hu, Z.Zhang, and T.G.Wensel (2003).
Activation of RGS9-1GTPase acceleration by its membrane anchor, R9AP.
  J Biol Chem, 278, 14550-14554.  
12517447 J.Cherfils, and M.Chabre (2003).
Activation of G-protein Galpha subunits by receptors through Galpha-Gbeta and Galpha-Ggamma interactions.
  Trends Biochem Sci, 28, 13-17.  
13678959 K.D.Ridge, N.G.Abdulaev, M.Sousa, and K.Palczewski (2003).
Phototransduction: crystal clear.
  Trends Biochem Sci, 28, 479-487.  
12860983 K.Wakasugi, T.Nakano, and I.Morishima (2003).
Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor.
  J Biol Chem, 278, 36505-36512.  
14623969 M.E.Hatley, S.W.Lockless, S.K.Gibson, A.G.Gilman, and R.Ranganathan (2003).
Allosteric determinants in guanine nucleotide-binding proteins.
  Proc Natl Acad Sci U S A, 100, 14445-14450.  
14622106 M.Natochin, and N.O.Artemyev (2003).
A point mutation uncouples transducin-alpha from the photoreceptor RGS and effector proteins.
  J Neurochem, 87, 1262-1271.  
12427730 R.Sterne-Marr, J.J.Tesmer, P.W.Day, R.P.Stracquatanio, J.A.Cilente, K.E.O'Connor, A.N.Pronin, J.L.Benovic, and P.B.Wedegaertner (2003).
G protein-coupled receptor Kinase 2/G alpha q/11 interaction. A novel surface on a regulator of G protein signaling homology domain for binding G alpha subunits.
  J Biol Chem, 278, 6050-6058.  
12531899 S.B.Hooks, G.L.Waldo, J.Corbitt, E.T.Bodor, A.M.Krumins, and T.K.Harden (2003).
RGS6, RGS7, RGS9, and RGS11 stimulate GTPase activity of Gi family G-proteins with differential selectivity and maximal activity.
  J Biol Chem, 278, 10087-10093.  
12559385 T.Wieland, and C.Mittmann (2003).
Regulators of G-protein signalling: multifunctional proteins with impact on signalling in the cardiovascular system.
  Pharmacol Ther, 97, 95.  
12525488 Z.Chen, W.D.Singer, C.D.Wells, S.R.Sprang, and P.C.Sternweis (2003).
Mapping the Galpha13 binding interface of the rgRGS domain of p115RhoGEF.
  J Biol Chem, 278, 9912-9919.  
12119397 G.Hu, and T.G.Wensel (2002).
R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein, RGS9-1.
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Shedding light on adaptation.
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Noncatalytic domains of RGS9-1.Gbeta 5L play a decisive role in establishing its substrate specificity.
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Signal-dependent translocation of transducin, RGS9-1-Gbeta5L complex, and arrestin to detergent-resistant membrane rafts in photoreceptors.
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Regulation of photoreceptor phosphodiesterase (PDE6) by phosphorylation of its inhibitory gamma subunit re-evaluated.
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Mutations in the carboxyl-terminal domain of phospholipase C-beta 1 delineate the dimer interface and a potential Galphaq interaction site.
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Evolutionary predictions of binding surfaces and interactions.
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Specific binding of RGS9-Gbeta 5L to protein anchor in photoreceptor membranes greatly enhances its catalytic activity.
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Regulators of G-protein signalling as new central nervous system drug targets.
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Rhodopsin: insights from recent structural studies.
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Structure of rhodopsin and the superfamily of seven-helical receptors: the same and not the same.
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G proteins and phototransduction.
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The guanine nucleotide-binding switch in three dimensions.
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Structure of the rgRGS domain of p115RhoGEF.
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PDB code: 1iap
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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