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Volumn 50, Issue 12, 2011, Pages 2223-2234

Binding between a Distal C-terminus fragment of cannabinoid receptor 1 and arrestin-2

Author keywords

[No Author keywords available]

Indexed keywords

ARRESTINS; C-TERMINUS; CANNABINOID RECEPTORS; CYTOSOLIC PROTEINS; DATA DRIVEN; DOCKING PROGRAMS; G PROTEIN COUPLED RECEPTORS; ISOTHERMAL TITRATION CALORIMETRY; LOOP CONFORMATION; PHOSPHOPEPTIDES; PHOSPHORYLATED PEPTIDES; POSITIVELY CHARGED; STRUCTURAL FACTOR;

EID: 79952926392     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1018144     Document Type: Article
Times cited : (18)

References (74)
  • 2
    • 0028924619 scopus 로고
    • Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin
    • Gurevich, V. V. and Benovic, J. L. (1995) Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin J. Biol. Chem. 270, 6010-6016
    • (1995) J. Biol. Chem. , vol.270 , pp. 6010-6016
    • Gurevich, V.V.1    Benovic, J.L.2
  • 4
    • 0026640659 scopus 로고
    • Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems
    • Lohse, M. J., Andexinger, S., Pitcher, J., Trukawinski, S., Codina, J., Faure, J. P., Caron, M. G., and Lefkowitz, R. J. (1992) Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems J. Biol. Chem. 267, 8558-8564
    • (1992) J. Biol. Chem. , vol.267 , pp. 8558-8564
    • Lohse, M.J.1    Andexinger, S.2    Pitcher, J.3    Trukawinski, S.4    Codina, J.5    Faure, J.P.6    Caron, M.G.7    Lefkowitz, R.J.8
  • 7
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz, R. J. and Shenoy, S. K. (2005) Transduction of receptor signals by beta-arrestins Science 308, 512-517
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 8
    • 0029054965 scopus 로고
    • Agonist-receptor efficacy. II. Agonist trafficking of receptor signals
    • Kenakin, T. (1995) Agonist-receptor efficacy. II. Agonist trafficking of receptor signals Trends Pharmacol. Sci. 16, 232-238
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 232-238
    • Kenakin, T.1
  • 10
    • 0036208442 scopus 로고    scopus 로고
    • Side-chain substitutions within angiotensin II reveal different requirements for signaling, internalization, and phosphorylation of type 1A angiotensin receptors
    • DOI 10.1124/mol.61.4.768
    • Holloway, A. C., Qian, H., Pipolo, L., Ziogas, J., Miura, S., Karnik, S., Southwell, B. R., Lew, M. J., and Thomas, W. G. (2002) Side-chain substitutions within angiotensin II reveal different requirements for signaling, internalization, and phosphorylation of type 1A angiotensin receptors Mol. Pharmacol. 61, 768-777 (Pubitemid 34273156)
    • (2002) Molecular Pharmacology , vol.61 , Issue.4 , pp. 768-777
    • Holloway, A.C.1    Qian, H.2    Pipolo, L.3    Ziogas, J.4    Miura, S.-I.5    Karnik, S.6    Southwell, B.R.7    Lew, M.J.8    Thomas, W.G.9
  • 12
    • 34447649922 scopus 로고    scopus 로고
    • Beta-arrestin-biased ligands at seven-transmembrane receptors
    • Violin, J. D. and Lefkowitz, R. J. (2007) Beta-arrestin-biased ligands at seven-transmembrane receptors Trends Pharmacol. Sci. 28, 416-422
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 416-422
    • Violin, J.D.1    Lefkowitz, R.J.2
  • 13
  • 15
    • 0842331059 scopus 로고    scopus 로고
    • The molecular acrobatics of arrestin activation
    • DOI 10.1016/j.tips.2003.12.008
    • Gurevich, V. V. and Gurevich, E. V. (2004) The molecular acrobatics of arrestin activation Trends Pharmacol. Sci. 25, 105-111 (Pubitemid 38183397)
    • (2004) Trends in Pharmacological Sciences , vol.25 , Issue.2 , pp. 105-111
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 16
    • 33646414189 scopus 로고    scopus 로고
    • The structural basis of arrestin-mediated regulation of G-protein-coupled receptors
    • Gurevich, V. V. and Gurevich, E. V. (2006) The structural basis of arrestin-mediated regulation of G-protein-coupled receptors Pharmacol. Ther. 110, 465-502
    • (2006) Pharmacol. Ther. , vol.110 , pp. 465-502
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 17
    • 0032568021 scopus 로고    scopus 로고
    • X-ray crystal structure of arrestin from bovine rod outer segments
    • DOI 10.1038/36147
    • Granzin, J., Wilden, U., Choe, H. W., Labahn, J., Krafft, B., and Buldt, G. (1998) X-ray crystal structure of arrestin from bovine rod outer segments Nature 391, 918-921 (Pubitemid 28157673)
    • (1998) Nature , vol.391 , Issue.6670 , pp. 918-921
    • Granzin, J.1    Wilden, U.2    Choe, H.-W.3    Labahn, J.4    Krafft, B.5    Buldt, G.6
  • 18
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of β-arrestin at 1.9 Å: Possible mechanism of receptor binding and membrane translocation
    • DOI 10.1016/S0969-2126(01)00644-X, PII S096921260100644X
    • Han, M., Gurevich, V. V., Vishnivetskiy, S. A., Sigler, P. B., and Schubert, C. (2001) Crystal structure of beta-arrestin at 1.9 Å: Possible mechanism of receptor binding and membrane translocation Structure 9, 869-880 (Pubitemid 32913504)
    • (2001) Structure , vol.9 , Issue.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 19
    • 0033574274 scopus 로고    scopus 로고
    • The 2.8 Å crystal structure of visual arrestin: A model for arrestin's regulation
    • Hirsch, J. A., Schubert, C., Gurevich, V. V., and Sigler, P. B. (1999) The 2.8 Å crystal structure of visual arrestin: A model for arrestin's regulation Cell 97, 257-269
    • (1999) Cell , vol.97 , pp. 257-269
    • Hirsch, J.A.1    Schubert, C.2    Gurevich, V.V.3    Sigler, P.B.4
  • 20
    • 33646942810 scopus 로고    scopus 로고
    • Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding
    • DOI 10.1074/jbc.M512703200
    • Milano, S. K., Kim, Y. M., Stefano, F. P., Benovic, J. L., and Brenner, C. (2006) Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding J. Biol. Chem. 281, 9812-9823 (Pubitemid 43864700)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9812-9823
    • Milano, S.K.1    Kim, Y.-M.2    Stefano, F.P.3    Benovic, J.L.4    Brenner, C.5
  • 21
    • 0037066145 scopus 로고    scopus 로고
    • Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis
    • DOI 10.1021/bi015905j
    • Milano, S. K., Pace, H. C., Kim, Y. M., Brenner, C., and Benovic, J. L. (2002) Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis Biochemistry 41, 3321-3328 (Pubitemid 34214030)
    • (2002) Biochemistry , vol.41 , Issue.10 , pp. 3321-3328
    • Milano, S.K.1    Pace, H.C.2    Kim, Y.-M.3    Brenner, C.4    Benovic, J.L.5
  • 23
    • 0027241013 scopus 로고
    • Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin
    • Gurevich, V. V. and Benovic, J. L. (1993) Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin J. Biol. Chem. 268, 11628-11638 (Pubitemid 23168111)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.16 , pp. 11628-11638
    • Gurevich, V.V.1    Benovic, J.L.2
  • 25
    • 0037088654 scopus 로고    scopus 로고
    • Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus
    • DOI 10.1074/jbc.M111086200
    • Potter, R. M., Key, T. A., Gurevich, V. V., Sklar, L. A., and Prossnitz, E. R. (2002) Arrestin variants display differential binding characteristics for the phosphorylated n-formyl peptide receptor carboxyl terminus J. Biol. Chem. 277, 8970-8978 (Pubitemid 34952969)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8970-8978
    • Potter, R.M.1    Alexander Key, T.2    Gurevich, V.V.3    Sklar, L.A.4    Prossnitz, E.R.5
  • 26
    • 33645524290 scopus 로고    scopus 로고
    • The differential engagement of arrestin surface charges by the various functional forms of the receptor
    • DOI 10.1074/jbc.M512148200
    • Hanson, S. M. and Gurevich, V. V. (2006) The differential engagement of arrestin surface charges by the various functional forms of the receptor J. Biol. Chem. 281, 3458-3462 (Pubitemid 43845961)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3458-3462
    • Hanson, S.M.1    Gurevich, V.V.2
  • 28
    • 0034731304 scopus 로고    scopus 로고
    • An additional phosphate-binding element in arrestin molecule: Implications for the mechanism of arrestin activation
    • DOI 10.1074/jbc.M007159200
    • Vishnivetskiy, S. A., Schubert, C., Climaco, G. C., Gurevich, Y. V., Velez, M. G., and Gurevich, V. V. (2000) An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation J. Biol. Chem. 275, 41049-41057 (Pubitemid 32054932)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.52 , pp. 41049-41057
    • Vishnivetskiy, S.A.1    Schubert, C.2    Climaco, G.C.3    Gurevich, Y.V.4    Velez, M.-G.5    Gurevich, V.V.6
  • 29
    • 6344255375 scopus 로고    scopus 로고
    • Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions
    • DOI 10.1074/jbc.M407341200
    • Kisselev, O. G., Downs, M. A., McDowell, J. H., and Hargrave, P. A. (2004) Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions J. Biol. Chem. 279, 51203-51207 (Pubitemid 40017863)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 51203-51207
    • Kisselev, O.G.1    Downs, M.A.2    McDowell, J.H.3    Hargrave, P.A.4
  • 30
    • 1942468184 scopus 로고    scopus 로고
    • The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin
    • DOI 10.1016/S0014-5793(04)00226-1, PII S0014579304002261
    • Kisselev, O. G., McDowell, J. H., and Hargrave, P. A. (2004) The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin FEBS Lett. 564, 307-311 (Pubitemid 38520938)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 307-311
    • Kisselev, O.G.1    McDowell, J.H.2    Hargrave, P.A.3
  • 31
    • 77950692040 scopus 로고    scopus 로고
    • Enhancement of endocannabinoid signaling by fatty acid amide hydrolase inhibition: A neuroprotective therapeutic modality
    • Hwang, J., Adamson, C., Butler, D., Janero, D. R., Makriyannis, A., and Bahr, B. A. (2010) Enhancement of endocannabinoid signaling by fatty acid amide hydrolase inhibition: A neuroprotective therapeutic modality Life Sci. 86, 615-623
    • (2010) Life Sci. , vol.86 , pp. 615-623
    • Hwang, J.1    Adamson, C.2    Butler, D.3    Janero, D.R.4    Makriyannis, A.5    Bahr, B.A.6
  • 36
    • 0032246648 scopus 로고    scopus 로고
    • Dual activation and inhibition of adenylyl cyclase by cannabinoid receptor agonists: Evidence for agonist-specific trafficking of intracellular responses
    • Bonhaus, D. W., Chang, L. K., Kwan, J., and Martin, G. R. (1998) Dual activation and inhibition of adenylyl cyclase by cannabinoid receptor agonists: Evidence for agonist-specific trafficking of intracellular responses J. Pharmacol. Exp. Ther. 287, 884-888 (Pubitemid 29131596)
    • (1998) Journal of Pharmacology and Experimental Therapeutics , vol.287 , Issue.3 , pp. 884-888
    • Bonhaus, D.W.1    Chang, L.K.2    Kwan, J.3    Martin, G.R.4
  • 37
    • 23044456227 scopus 로고    scopus 로고
    • Interaction and structural study of kinin peptide bradykinin and ganglioside monosialylated 1 micelle
    • DOI 10.1002/bip.20278
    • Chatterjee, C. and Mukhopadhyay, C. (2005) Interaction and structural study of kinin peptide bradykinin and ganglioside monosialylated 1 micelle Biopolymers 78, 197-205 (Pubitemid 41140774)
    • (2005) Biopolymers , vol.78 , Issue.4 , pp. 197-205
    • Chatterjee, C.1    Mukhopadhyay, C.2
  • 38
    • 3042780243 scopus 로고    scopus 로고
    • Identification of a potent and highly efficacious, yet slowly desensitizing CB1 cannabinoid receptor agonist
    • DOI 10.1038/sj.bjp.0705792
    • Luk, T., Jin, W., Zvonok, A., Lu, D., Lin, X. Z., Chavkin, C., Makriyannis, A., and Mackie, K. (2004) Identification of a potent and highly efficacious, yet slowly desensitizing CB1 cannabinoid receptor agonist Br. J. Pharmacol. 142, 495-500 (Pubitemid 38869863)
    • (2004) British Journal of Pharmacology , vol.142 , Issue.3 , pp. 495-500
    • Luk, T.1    Jin, W.2    Zvonok, A.3    Lu, D.4    Lin, X.-Z.5    Chavkin, C.6    Makriyannis, A.7    Mackie, K.8
  • 40
    • 0032771955 scopus 로고    scopus 로고
    • Internalization and recycling of the CB1 cannabinoid receptor
    • DOI 10.1046/j.1471-4159.1999.0730493.x
    • Hsieh, C., Brown, S., Derleth, C., and Mackie, K. (1999) Internalization and recycling of the CB1 cannabinoid receptor J. Neurochem. 73, 493-501 (Pubitemid 29339821)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.2 , pp. 493-501
    • Hsieh, C.1    Brown, S.2    Derleth, C.3    Mackie, K.4
  • 41
    • 45249083370 scopus 로고    scopus 로고
    • 1 cannabinoid receptor internalization by a promiscuous phosphorylation-dependent mechanism
    • DOI 10.1111/j.1471-4159.2008.05336.x
    • Daigle, T. L., Kwok, M. L., and Mackie, K. (2008) Regulation of CB1 cannabinoid receptor internalization by a promiscuous phosphorylation-dependent mechanism J. Neurochem. 106, 70-82 (Pubitemid 351840192)
    • (2008) Journal of Neurochemistry , vol.106 , Issue.1 , pp. 70-82
    • Daigle, T.L.1    Kwok, M.L.2    Mackie, K.3
  • 42
    • 37349043924 scopus 로고    scopus 로고
    • 1 cannabinoid receptor desensitization defines the time course of ERK1/2 MAP kinase signaling
    • DOI 10.1016/j.neuropharm.2007.06.005, PII S0028390807001712, Cannabinoid Signaling in the Nervous system
    • Daigle, T. L., Kearn, C. S., and Mackie, K. (2008) Rapid CB1 cannabinoid receptor desensitization defines the time course of ERK1/2 map kinase signaling Neuropharmacology 54, 36-44 (Pubitemid 350299401)
    • (2008) Neuropharmacology , vol.54 , Issue.1 , pp. 36-44
    • Daigle, T.L.1    Kearn, C.S.2    Mackie, K.3
  • 44
    • 12844283365 scopus 로고    scopus 로고
    • The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism
    • DOI 10.1016/j.bbamem.2004.10.011, PII S0005273604002810
    • Choi, G., Guo, J., and Makriyannis, A. (2005) The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism Biochim. Biophys. Acta 1668, 1-9 (Pubitemid 40164727)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1668 , Issue.1 , pp. 1-9
    • Choi, G.1    Guo, J.2    Makriyannis, A.3
  • 49
    • 74549177146 scopus 로고    scopus 로고
    • Role of helix 8 of the thyrotropin-releasing hormone receptor in phosphorylation by G protein-coupled receptor kinase
    • Gehret, A. U., Jones, B. W., Tran, P. N., Cook, L. B., Greuber, E. K., and Hinkle, P. M. (2010) Role of helix 8 of the thyrotropin-releasing hormone receptor in phosphorylation by G protein-coupled receptor kinase Mol. Pharmacol. 77, 288-297
    • (2010) Mol. Pharmacol. , vol.77 , pp. 288-297
    • Gehret, A.U.1    Jones, B.W.2    Tran, P.N.3    Cook, L.B.4    Greuber, E.K.5    Hinkle, P.M.6
  • 51
    • 65249115932 scopus 로고    scopus 로고
    • Solid-state NMR and molecular dynamics characterization of cannabinoid receptor-1 (CB1) helix 7 conformational plasticity in model membranes
    • Tiburu, E. K., Bowman, A. L., Struppe, J. O., Janero, D. R., Avraham, H. K., and Makriyannis, A. (2009) Solid-state NMR and molecular dynamics characterization of cannabinoid receptor-1 (CB1) helix 7 conformational plasticity in model membranes Biochim. Biophys. Acta 1788, 1159-1167
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1159-1167
    • Tiburu, E.K.1    Bowman, A.L.2    Struppe, J.O.3    Janero, D.R.4    Avraham, H.K.5    Makriyannis, A.6
  • 52
    • 70449715120 scopus 로고    scopus 로고
    • NMR solution structure of human cannabinoid receptor-1 helix 7/8 peptide: Candidate electrostatic interactions and microdomain formation
    • (2009), - 446
    • Tyukhtenko, S., Tiburu, E. K., Deshmukh, L., Vinogradova, O., Janero, D. R., and Makriyannis, A. (2009) NMR solution structure of human cannabinoid receptor-1 helix 7/8 peptide: Candidate electrostatic interactions and microdomain formation, Biochem. Biophys. Res. Commun. 390, 441 - 446.
    • Biochem. Biophys. Res. Commun. , vol.390 , pp. 441
    • Tyukhtenko, S.1    Tiburu, E.K.2    Deshmukh, L.3    Vinogradova, O.4    Janero, D.R.5    Makriyannis, A.6
  • 53
    • 68349132226 scopus 로고    scopus 로고
    • Structural analysis of the human cannabinoid receptor one carboxyl-terminus identifies two amphipathic helices
    • Ahn, K. H., Pellegrini, M., Tsomaia, N., Yatawara, A. K., Kendall, D. A., and Mierke, D. F. (2009) Structural analysis of the human cannabinoid receptor one carboxyl-terminus identifies two amphipathic helices Biopolymers 91, 565-573
    • (2009) Biopolymers , vol.91 , pp. 565-573
    • Ahn, K.H.1    Pellegrini, M.2    Tsomaia, N.3    Yatawara, A.K.4    Kendall, D.A.5    Mierke, D.F.6
  • 54
    • 34948829679 scopus 로고    scopus 로고
    • Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2
    • DOI 10.1016/j.febslet.2007.09.030, PII S0014579307010125
    • Bakshi, K., Mercier, R. W., and Pavlopoulos, S. (2007) Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2 FEBS Lett. 581, 5009-5016 (Pubitemid 47531768)
    • (2007) FEBS Letters , vol.581 , Issue.25 , pp. 5009-5016
    • Bakshi, K.1    Mercier, R.W.2    Pavlopoulos, S.3
  • 56
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. and Ernst, R. R. (1983) Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy J. Magn. Reson. 53, 521-528
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 57
    • 45449123980 scopus 로고
    • Iterative schemes for bilinear operators; Application to spin decoupling
    • Shaka, A. J., Lee, C. J., and Pines, A. (1988) Iterative schemes for bilinear operators; application to spin decoupling J. Magn. Reson., B 77, 274-293
    • (1988) J. Magn. Reson., B , vol.77 , pp. 274-293
    • Shaka, A.J.1    Lee, C.J.2    Pines, A.3
  • 58
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J. Biomol. NMR 2, 661-665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 59
    • 0029400480 scopus 로고
    • NMRpipe: A multidimensional spectral processing system based on Unix pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRpipe: A multidimensional spectral processing system based on Unix pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 61
    • 0023008905 scopus 로고
    • Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination: A model study of crambin
    • DOI 10.1016/0022-2836(86)90146-4
    • Clore, G. M., Brunger, A. T., Karplus, M., and Gronenborn, A. M. (1986) Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin J. Mol. Biol. 191, 523-551 (Pubitemid 17187239)
    • (1986) Journal of Molecular Biology , vol.191 , Issue.3 , pp. 523-551
    • Clore, G.M.1    Brunger, A.T.2    Karplus, M.3    Gronenborn, A.M.4
  • 62
    • 0000939457 scopus 로고
    • The three-dimensional structure of alpha1-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore, G. M., Nilges, M., Sukumaran, D. K., Brunger, A. T., Karplus, M., and Gronenborn, A. M. (1986) The three-dimensional structure of alpha1-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics EMBO J. 5, 2729-2735
    • (1986) EMBO J. , vol.5 , pp. 2729-2735
    • Clore, G.M.1    Nilges, M.2    Sukumaran, D.K.3    Brunger, A.T.4    Karplus, M.5    Gronenborn, A.M.6
  • 63
    • 0023475020 scopus 로고
    • Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, G. M., Gronenborn, A. M., Nilges, M., and Ryan, C. A. (1987) Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics Biochemistry 26, 8012-8023
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 64
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner, G., Braun, W., Havel, T. F., Schaumann, T., Go, N., and Wuthrich, K. (1987) Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN J. Mol. Biol. 196, 611-639
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wuthrich, K.6
  • 65
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A. T. (2007) Version 1.2 of the crystallography and NMR system Nat. Protoc. 2, 2728-2733
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 69
    • 0000243829 scopus 로고
    • PROCHECK-A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK-A program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 70
    • 0035742163 scopus 로고    scopus 로고
    • The vmd-xplor visualization package for NMR structure refinement
    • Schwieters, C. D. and Clore, G. M. (2001) The vmd-xplor visualization package for NMR structure refinement J. Magn. Reson. 149, 239-244
    • (2001) J. Magn. Reson. , vol.149 , pp. 239-244
    • Schwieters, C.D.1    Clore, G.M.2
  • 71
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • DOI 10.1021/ja026939x
    • Dominguez, C., Boelens, R., and Bonvin, A. M. (2003) HADDOCK: A protein-protein docking approach based on biochemical or biophysical information J. Am. Chem. Soc. 125, 1731-1737 (Pubitemid 36232568)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 72
    • 0347723912 scopus 로고    scopus 로고
    • Mapping the arrestin-receptor interface: Structural elements responsible for receptor specificity of arrestin proteins
    • DOI 10.1074/jbc.M308834200
    • Vishnivetskiy, S. A., Hosey, M. M., Benovic, J. L., and Gurevich, V. V. (2004) Mapping the arrestin-receptor interface-Structural elements responsible for receptor specificity of arrestin proteins J. Biol. Chem. 279, 1262-1268 (Pubitemid 38082650)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1262-1268
    • Vishnivetskiy, S.A.1    Hosey, M.M.2    Benovic, J.L.3    Gurevich, V.V.4
  • 73
    • 79952941480 scopus 로고
    • NACCESS, 2.1.1 ed., Department of Biochemistry and Molecular Biology, University College, London
    • Hubbard, S. and Thornton, J. (1993) NACCESS, 2.1.1 ed., Department of Biochemistry and Molecular Biology, University College, London.
    • (1993)
    • Hubbard, S.1    Thornton, J.2
  • 74
    • 0000393431 scopus 로고
    • The two-dimensional transferred nuclear overhauser effect
    • Clore, G. M. and Gronenborn, A. M. (1982) The two-dimensional transferred nuclear overhauser effect J. Magn. Reson. 48, 402-417
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2


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