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Volumn 5, Issue , 2014, Pages

Crystal structure of a common GPCR-binding interface for G protein and arrestin

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; RETINA S ANTIGEN; RHODOPSIN;

EID: 84916610476     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5801     Document Type: Article
Times cited : (139)

References (61)
  • 1
    • 70350362562 scopus 로고    scopus 로고
    • A G protein-coupled receptor at work: The rhodopsin model
    • Hofmann, K. P. et al. A G protein-coupled receptor at work: the rhodopsin model. Trends Biochem. Sci. 34, 540-552 (2009).
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 540-552
    • Hofmann, K.P.1
  • 2
    • 0032516098 scopus 로고    scopus 로고
    • Light-activated rhodopsin induces structural binding motif in G protein alpha subunit
    • Kisselev, O. G. et al. Light-activated rhodopsin induces structural binding motif in G protein alpha subunit. Proc. Natl Acad. Sci. USA 95, 4270-4275 (1998) .
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4270-4275
    • Kisselev, O.G.1
  • 3
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Scheerer, P. et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455, 497-502 (2008).
    • (2008) Nature , vol.455 , pp. 497-502
    • Scheerer, P.1
  • 4
    • 79953234218 scopus 로고    scopus 로고
    • Crystal structure of metarhodopsin II
    • Choe, H. W. et al. Crystal structure of metarhodopsin II. Nature 471, 651-655 (2011) .
    • (2011) Nature , vol.471 , pp. 651-655
    • Choe, H.W.1
  • 5
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the beta2 adrenergic receptor-Gs protein complex
    • Rasmussen, S. G. et al. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1
  • 6
    • 84855990615 scopus 로고    scopus 로고
    • Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II
    • Deupi, X. et al. Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proc. Natl Acad. Sci. USA 109, 119-124 (2012) .
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 119-124
    • Deupi, X.1
  • 7
    • 84855854548 scopus 로고    scopus 로고
    • Photoreceptor signaling: Supporting vision across a wide range of light intensities
    • Arshavsky, V. Y. & Burns, M. E. Photoreceptor signaling: supporting vision across a wide range of light intensities. J. Biol. Chem. 287, 1620-1626 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 1620-1626
    • Arshavsky, V.Y.1    Burns, M.E.2
  • 8
    • 0033574274 scopus 로고    scopus 로고
    • The 2.8 A crystal structure of visual arrestin: A model for arrestin's regulation
    • Hirsch, J. A., Schubert, C., Gurevich, V. V. & Sigler, P. B. The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell 97, 257-269 (1999) .
    • (1999) Cell , vol.97 , pp. 257-269
    • Hirsch, J.A.1    Schubert, C.2    Gurevich, V.V.3    Sigler, P.B.4
  • 9
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of beta-arrestin at 1.9 A: Possible mechanism of receptor binding and membrane Translocation
    • Han, M., Gurevich, V. V., Vishnivetskiy, S. A., Sigler, P. B. & Schubert, C. Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. Structure 9, 869-880 (2001).
    • (2001) Structure , vol.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 10
    • 28144443994 scopus 로고    scopus 로고
    • Crystal structure of cone arrestin at 2.3A: Evolution of receptor specificity
    • Sutton, R. B. et al. Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. J. Mol. Biol. 354, 1069-1080 (2005).
    • (2005) J. Mol. Biol. , vol.354 , pp. 1069-1080
    • Sutton, R.B.1
  • 11
    • 79551687952 scopus 로고    scopus 로고
    • Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes
    • Zhan, X., Gimenez, L. E., Gurevich, V. V. & Spiller, B. W. Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J. Mol. Biol. 406, 467-478 (2011).
    • (2011) J. Mol. Biol. , vol.406 , pp. 467-478
    • Zhan, X.1    Gimenez, L.E.2    Gurevich, V.V.3    Spiller, B.W.4
  • 12
    • 84877581910 scopus 로고    scopus 로고
    • Crystal structure of pre-activated arrestin p44
    • Kim, Y. J. et al. Crystal structure of pre-activated arrestin p44. Nature 497, 142-146 (2013).
    • (2013) Nature , vol.497 , pp. 142-146
    • Kim, Y.J.1
  • 13
    • 84877581626 scopus 로고    scopus 로고
    • Structure of active beta-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide
    • Shukla, A. K. et al. Structure of active beta-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497, 137-141 (2013).
    • (2013) Nature , vol.497 , pp. 137-141
    • Shukla, A.K.1
  • 14
    • 33645506641 scopus 로고    scopus 로고
    • Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin
    • Hanson, S. M. et al. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc. Natl Acad. Sci. USA 103, 4900-4905 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4900-4905
    • Hanson, S.M.1
  • 15
    • 34548490297 scopus 로고    scopus 로고
    • Dynamics of arrestin-rhodopsin interactions: Loop movement is involved in arrestin activation and receptor binding
    • Sommer, M. E., Farrens, D. L., McDowell, J. H., Weber, L. A. & Smith, W. C. Dynamics of arrestin-rhodopsin interactions: loop movement is involved in arrestin activation and receptor binding. J. Biol. Chem. 282, 25560-25568 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 25560-25568
    • Sommer, M.E.1    Farrens, D.L.2    McDowell, J.H.3    Weber, L.A.4    Smith, W.C.5
  • 16
    • 84868573187 scopus 로고    scopus 로고
    • Conformation of receptor-bound visual arrestin
    • Kim, M. et al. Conformation of receptor-bound visual arrestin. Proc. Natl Acad. Sci. USA 109, 18407-18412 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 18407-18412
    • Kim, M.1
  • 18
    • 84872529567 scopus 로고    scopus 로고
    • Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin
    • Zhuang, T. et al. Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc. Natl Acad. Sci. USA 110, 942-947 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.110 , pp. 942-947
    • Zhuang, T.1
  • 19
    • 84901472810 scopus 로고    scopus 로고
    • Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: Evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding
    • Sinha, A., Jones Brunette, A. M., Fay, J. F., Schafer, C. T. & Farrens, D. L. Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding. Biochemistry 53, 3294-3307 (2014).
    • (2014) Biochemistry , vol.53 , pp. 3294-3307
    • Sinha, A.1    Jones Brunette, A.M.2    Fay, J.F.3    Schafer, C.T.4    Farrens, D.L.5
  • 20
    • 84885448271 scopus 로고    scopus 로고
    • Opsin, a structural model for olfactory receptors?
    • Park, J. H. et al. Opsin, a structural model for olfactory receptors? Angewandte Chemie. 52, 11021-11024 (2013).
    • (2013) Angewandte Chemie. , vol.52 , pp. 11021-11024
    • Park, J.H.1
  • 21
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H. W. & Ernst, O. P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454, 183-187 (2008).
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 22
    • 79953242234 scopus 로고    scopus 로고
    • The structural basis of agonist-induced activation in constitutively active rhodopsin
    • Standfuss, J. et al. The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 471, 656-660 (2011).
    • (2011) Nature , vol.471 , pp. 656-660
    • Standfuss, J.1
  • 23
    • 70449591430 scopus 로고    scopus 로고
    • Helix formation in arrestin accompanies recognition of photoactivated rhodopsin
    • Feuerstein, S. E. et al. Helix formation in arrestin accompanies recognition of photoactivated rhodopsin. Biochemistry 48, 10733-10742 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10733-10742
    • Feuerstein, S.E.1
  • 24
    • 0033586719 scopus 로고    scopus 로고
    • Binding of arrestin to cytoplasmic loop mutants of bovine rhodopsin
    • Raman, D., Osawa, S. & Weiss, E. R. Binding of arrestin to cytoplasmic loop mutants of bovine rhodopsin. Biochemistry 38, 5117-5123 (1999).
    • (1999) Biochemistry , vol.38 , pp. 5117-5123
    • Raman, D.1    Osawa, S.2    Weiss, E.R.3
  • 25
    • 33646365380 scopus 로고    scopus 로고
    • A beta-arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors
    • Marion, S., Oakley, R. H., Kim, K. M., Caron, M. G. & Barak, L. S. A beta-arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors. J. Biol. Chem. 281, 2932-2938 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 2932-2938
    • Marion, S.1    Oakley, R.H.2    Kim, K.M.3    Caron, M.G.4    Barak, L.S.5
  • 26
    • 58849087235 scopus 로고    scopus 로고
    • An intracellular loop 2 amino acid residue determines differential binding of arrestin to the dopamine D2 and D3 receptors
    • Lan, H., Teeter, M. M., Gurevich, V. V. & Neve, K. A. An intracellular loop 2 amino acid residue determines differential binding of arrestin to the dopamine D2 and D3 receptors. Mol. Pharmacol. 75, 19-26 (2009).
    • (2009) Mol. Pharmacol. , vol.75 , pp. 19-26
    • Lan, H.1    Teeter, M.M.2    Gurevich, V.V.3    Neve, K.A.4
  • 27
    • 84860201432 scopus 로고    scopus 로고
    • Structural insights into biased G protein-coupled receptor signaling revealed by fluorescence spectroscopy
    • Rahmeh, R. et al. Structural insights into biased G protein-coupled receptor signaling revealed by fluorescence spectroscopy. Proc. Natl Acad. Sci. USA 109, 6733-6738 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 6733-6738
    • Rahmeh, R.1
  • 28
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR
    • Liu, J. J., Horst, R., Katritch, V., Stevens, R. C. & Wuthrich, K. Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR. Science 335, 1106-1110 (2012).
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wuthrich, K.5
  • 29
    • 84877631485 scopus 로고    scopus 로고
    • Structural features for functional selectivity at serotonin receptors
    • Wacker, D. et al. Structural features for functional selectivity at serotonin receptors. Science 340, 615-619 (2013).
    • (2013) Science , vol.340 , pp. 615-619
    • Wacker, D.1
  • 30
    • 0024582884 scopus 로고
    • Binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II
    • Schleicher, A., Kuhn, H. & Hofmann, K. P. Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II. Biochemistry 28, 1770-1775 (1989).
    • (1989) Biochemistry , vol.28 , pp. 1770-1775
    • Schleicher, A.1    Kuhn, H.2    Kinetics, P.H.K.3
  • 31
    • 0023716027 scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit
    • Hamm, H. E. et al. Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit. Science 241, 832-835 (1988).
    • (1988) Science , vol.241 , pp. 832-835
    • Hamm, H.E.1
  • 32
    • 33846840831 scopus 로고    scopus 로고
    • Interaction of a G protein-coupled receptor with a G protein-derived peptide induces structural changes in both peptide and receptor: A Fourier-transform infrared study using isotopically labeled peptides
    • Vogel, R., Martell, S., Mahalingam, M., Engelhard, M. & Siebert, F. Interaction of a G protein-coupled receptor with a G protein-derived peptide induces structural changes in both peptide and receptor: a Fourier-transform infrared study using isotopically labeled peptides. J. Mol. Biol. 366, 1580-1588 (2007).
    • (2007) J. Mol. Biol. , vol.366 , pp. 1580-1588
    • Vogel, R.1    Martell, S.2    Mahalingam, M.3    Engelhard, M.4    Siebert, F.5
  • 33
    • 84883072253 scopus 로고    scopus 로고
    • Precision vs flexibility in GPCR signaling
    • Elgeti, M. et al. Precision vs flexibility in GPCR signaling. J. Am. Chem. Soc. 135, 12305-12312 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12305-12312
    • Elgeti, M.1
  • 34
    • 0020020855 scopus 로고
    • Preparation of retinal rod outer segments
    • Papermaster, D. S. Preparation of retinal rod outer segments. Methods Enzymol. 81, 48-52 (1982).
    • (1982) Methods Enzymol. , vol.81 , pp. 48-52
    • Papermaster, D.S.1
  • 35
    • 0034048307 scopus 로고    scopus 로고
    • Assays for activation of opsin by all-trans-retinal
    • Sachs, K., Maretzki, D. & Hofmann, K. P. Assays for activation of opsin by all-trans-retinal. Methods Enzymol. 315, 238-251 (2000).
    • (2000) Methods Enzymol. , vol.315 , pp. 238-251
    • Sachs, K.1    Maretzki, D.2    Hofmann, K.P.3
  • 36
    • 36048983801 scopus 로고    scopus 로고
    • Advances in spectroscopic methods for biological crystals. 1. Fluorescence lifetime measurements
    • Royant, A. et al. Advances in spectroscopic methods for biological crystals. 1. Fluorescence lifetime measurements. J. Appl. Crystallogr. 40, 1105-1112 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 1105-1112
    • Royant, A.1
  • 37
    • 84860140442 scopus 로고    scopus 로고
    • ID29: A high-intensity highly automated ESRF beamline for macromolecular crystallography experiments exploiting anomalous scattering
    • de Sanctis, D. et al. ID29: a high-intensity highly automated ESRF beamline for macromolecular crystallography experiments exploiting anomalous scattering. J Synchrotron Radiat. 19, 455-461 (2012).
    • (2012) J Synchrotron Radiat. , vol.19 , pp. 455-461
    • De Sanctis, D.1
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project, N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol Crystallogr. , vol.50 , pp. 760-763
  • 41
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol .Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol .Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 43
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N. & Murshudov, G. N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133 (2001).
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 44
    • 16644364842 scopus 로고    scopus 로고
    • REFMAC5 dictionary: Organization of prior chemical knowledge and guidelines for its use
    • Vagin, A. A. et al. REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr. D Biol. Crystallogr. 60, 2184-2195 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2184-2195
    • Vagin, A.A.1
  • 46
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J. & Wodak, S. J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55, 191-205 (1999).
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 47
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereo chemical quality of protein structures
    • Laskowski, R. A., Moss, D. S. & Thornton, J. M. Procheck: a program to check the stereo chemical quality of protein structures. J. Appl. Cryst. 26, 283-291 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 49
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by C alpha geometry: Phi,psi and C beta deviation
    • Lovell, S. C. et al. Structure validation by C alpha geometry: phi,psi and C beta deviation. Proteins 50, 437-450 (2003).
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1
  • 50
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K. & Thornton, J. M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777-793 (1994).
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 51
    • 80054911951 scopus 로고    scopus 로고
    • LigPlot +: Multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski, R. A. & Swindells, M. B. LigPlot +: multiple ligand-protein interaction diagrams for drug discovery. J. Chem. Informat. Model 51, 2778-2786 (2011).
    • (2011) J. Chem. Informat. Model , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 53
    • 77957055780 scopus 로고
    • Integrated methods for the construction of threedimensional models and computational probing of structure-function relations in G-protein coupled receptors
    • Ballesteros, J. A. & Weinstein, H. Integrated methods for the construction of threedimensional models and computational probing of structure-function relations in G-protein coupled receptors. Methods Neurosci. 25, 366-428 (1995).
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 54
    • 84866102271 scopus 로고    scopus 로고
    • Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin
    • Sommer, M. E., Hofmann, K. P. & Heck, M. Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin. Nat. Commun. 3, 995 (2012).
    • (2012) Nat. Commun. , vol.3 , pp. 995
    • Sommer, M.E.1    Hofmann, K.P.2    Heck, M.3
  • 55
    • 0021758996 scopus 로고
    • Temperature and pH dependence of the metarhodopsin I-metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions
    • Parkes, J. H. & Liebman, P. A. Temperature and pH dependence of the metarhodopsin I-metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions. Biochemistry 23, 5054-5061 (1984).
    • (1984) Biochemistry , vol.23 , pp. 5054-5061
    • Parkes, J.H.1    Liebman, P.A.2
  • 56
    • 33646899690 scopus 로고    scopus 로고
    • Dynamics of arrestin-rhodopsin interactions: Acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent
    • Sommer, M. E., Smith, W. C. & Farrens, D. L. Dynamics of arrestin-rhodopsin interactions: acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent. J. Biol. Chem. 281, 9407-9417 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 9407-9417
    • Sommer, M.E.1    Smith, W.C.2    Farrens, D.L.3
  • 57
    • 0034006773 scopus 로고    scopus 로고
    • Arrestin: Mutagenesis, expression, purification, and functional characterization
    • Gurevich, V. V. & Benovic, J. L. Arrestin: mutagenesis, expression, purification, and functional characterization. Methods Enzymol. 315, 422-437 (2000).
    • (2000) Methods Enzymol. , vol.315 , pp. 422-437
    • Gurevich, V.V.1    Benovic, J.L.2
  • 58
    • 79953213342 scopus 로고    scopus 로고
    • Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors
    • Sommer, M. E., Hofmann, K. P. & Heck, M. Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors. J. Biol. Chem. 286, 7359-7369 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 7359-7369
    • Sommer, M.E.1    Hofmann, K.P.2    Heck, M.3
  • 60
    • 0031600116 scopus 로고    scopus 로고
    • Rhodopsin: A prototypical G protein-coupled receptor
    • Sakmar, T. P. Rhodopsin: a prototypical G protein-coupled receptor. Progr. Nucleic Acid Res. Mol. Biol. 59, 1-34 (1998).
    • (1998) Progr. Nucleic Acid Res. Mol. Biol. , vol.59 , pp. 1-34
    • Sakmar . T, P.1
  • 61
    • 79955680725 scopus 로고    scopus 로고
    • Conserved Tyr223(5.58) plays different roles in the activation and G-protein interaction of rhodopsin
    • Elgeti, M., Kazmin, R., Heck, M., Morizumi, T. & Ritter, E. et al. Conserved Tyr223(5.58) plays different roles in the activation and G-protein interaction of rhodopsin. J. Am. Chem. Soc. 133, 7159-7165 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7159-7165
    • Elgeti, M.1    Kazmin, R.2    Heck, M.3    Morizumi, T.4    Ritter, E.5


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