메뉴 건너뛰기




Volumn 159, Issue 3, 2007, Pages 359-368

Unique helical conformation of the fourth cytoplasmic loop of the CB1 cannabinoid receptor in a negatively charged environment

Author keywords

Cell surface 7 transmembrane receptors; G protein coupled receptors; Signal transduction mechanisms; Sodium dodecyl sulfate (SDS) micelles; Two dimensional proton nuclear magnetic resonance (2D 1H NMR) spectroscopy

Indexed keywords

ARGINYLSERYLLYSYLASPARTYLLEUCYLARGINYLHISTIDYLALANYLPHENYLALANYLARGINYLSERYLMETHIONYLPHENYLALANYLPROLYLSERYLSERYLGLUTAMIC ACID; CANNABINOID 1 RECEPTOR; DODECYL SULFATE SODIUM; GUANINE NUCLEOTIDE BINDING PROTEIN; PEPTIDE; UNCLASSIFIED DRUG;

EID: 34548386281     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2007.04.004     Document Type: Article
Times cited : (14)

References (51)
  • 2
    • 0035951097 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix H8
    • Altenbach C., Cai K., Klein-Seetharaman J., Khorana H.G., and Hubbell W.L. Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix H8. Biochemistry 40 (2001) 15483-15492
    • (2001) Biochemistry , vol.40 , pp. 15483-15492
    • Altenbach, C.1    Cai, K.2    Klein-Seetharaman, J.3    Khorana, H.G.4    Hubbell, W.L.5
  • 3
    • 0035951062 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1
    • Altenbach C., Klein-Seetharaman J., Cai K., Khorana H.G., and Hubbell W.L. Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1. Biochemistry 40 (2001) 15493-15500
    • (2001) Biochemistry , vol.40 , pp. 15493-15500
    • Altenbach, C.1    Klein-Seetharaman, J.2    Cai, K.3    Khorana, H.G.4    Hubbell, W.L.5
  • 4
    • 48749148224 scopus 로고
    • Rattle: a velocity version of the shake algorithm for molecular dynamics calculations
    • Anderson H. Rattle: a velocity version of the shake algorithm for molecular dynamics calculations. J. Comp. Phys. 52 (1983) 24-34
    • (1983) J. Comp. Phys. , vol.52 , pp. 24-34
    • Anderson, H.1
  • 5
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., and Davis D. MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65 (1985) 355-360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.2
  • 6
    • 0000700103 scopus 로고
    • Time development of Nuclear Overhauser Effects in multispin systems
    • Bothner-By A.A., and Noggle J.H. Time development of Nuclear Overhauser Effects in multispin systems. J. Am. Chem. Soc. 101 (1979) 5152-5155
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5152-5155
    • Bothner-By, A.A.1    Noggle, J.H.2
  • 7
    • 0025119481 scopus 로고
    • Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance
    • Bradley E.K., Thomason J.F., Cohen F.E., Kosen P.A., and Kuntz I.D. Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance. J. Mol. Biol. 215 (1990) 607-622
    • (1990) J. Mol. Biol. , vol.215 , pp. 607-622
    • Bradley, E.K.1    Thomason, J.F.2    Cohen, F.E.3    Kosen, P.A.4    Kuntz, I.D.5
  • 8
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler L., and Ernst R.R. Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J. Magn. Reson. 53 (1983) 521-528
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 9
    • 12844283365 scopus 로고    scopus 로고
    • The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism
    • Choi G., Guo J., and Makriyannis A. The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism. Biochim. Biophys. Acta 1668 (2005) 1-9
    • (2005) Biochim. Biophys. Acta , vol.1668 , pp. 1-9
    • Choi, G.1    Guo, J.2    Makriyannis, A.3
  • 12
    • 46549093794 scopus 로고
    • Separation of chemical exchange and cross-relaxation effects in two-dimensional NMR spectroscopy
    • Davis D.G., and Bax A. Separation of chemical exchange and cross-relaxation effects in two-dimensional NMR spectroscopy. J. Magn. Reson. 64 (1985) 533-535
    • (1985) J. Magn. Reson. , vol.64 , pp. 533-535
    • Davis, D.G.1    Bax, A.2
  • 15
    • 0030976014 scopus 로고    scopus 로고
    • Structure of the C-terminal fragment 300-320 of the rat angiotensin II AT1A receptor and its relevance with respect to G-protein coupling
    • Franzoni L., Nicastro G., Pertinhez T.A., Tato M., Nakaie C.R., Paiva A.C., Schreier S., and Spisni A. Structure of the C-terminal fragment 300-320 of the rat angiotensin II AT1A receptor and its relevance with respect to G-protein coupling. J. Biol. Chem. 272 (1997) 9734-9741
    • (1997) J. Biol. Chem. , vol.272 , pp. 9734-9741
    • Franzoni, L.1    Nicastro, G.2    Pertinhez, T.A.3    Tato, M.4    Nakaie, C.R.5    Paiva, A.C.6    Schreier, S.7    Spisni, A.8
  • 16
    • 0001455550 scopus 로고    scopus 로고
    • Gradient-enhanced TOCSY experiments with improved sensitivity and solvent suppression
    • Fulton D.B., Hrabal R., and Ni F. Gradient-enhanced TOCSY experiments with improved sensitivity and solvent suppression. J. Biomol. NMR 8 (1996) 213-218
    • (1996) J. Biomol. NMR , vol.8 , pp. 213-218
    • Fulton, D.B.1    Hrabal, R.2    Ni, F.3
  • 17
    • 0031264537 scopus 로고    scopus 로고
    • ROESY with water flip back for high-field NMR of biomolecules
    • Fulton D.B., and Ni F. ROESY with water flip back for high-field NMR of biomolecules. J. Magn. Reson. 129 (1997) 93-97
    • (1997) J. Magn. Reson. , vol.129 , pp. 93-97
    • Fulton, D.B.1    Ni, F.2
  • 18
    • 0035017426 scopus 로고    scopus 로고
    • Molecular dynamics simulation of adrenocorticotropin (1-10) peptide in a solvated dodecylphosphocholine micelle
    • Gao X., and Wong T.C. Molecular dynamics simulation of adrenocorticotropin (1-10) peptide in a solvated dodecylphosphocholine micelle. Biopolymers 58 (2001) 643-659
    • (2001) Biopolymers , vol.58 , pp. 643-659
    • Gao, X.1    Wong, T.C.2
  • 19
    • 0035148377 scopus 로고    scopus 로고
    • NMR studies of adrenocorticotropin hormone peptides in sodium dodecyl sulfate and dodecylphosphocholine micelles: proline isomerism and interactions of the peptides with micelles
    • Gao X., and Wong T.C. NMR studies of adrenocorticotropin hormone peptides in sodium dodecyl sulfate and dodecylphosphocholine micelles: proline isomerism and interactions of the peptides with micelles. Biopolymers 58 (2001) 20-32
    • (2001) Biopolymers , vol.58 , pp. 20-32
    • Gao, X.1    Wong, T.C.2
  • 20
    • 33845378213 scopus 로고
    • Two-dimensional correlation of connected NMR transitions
    • Griesinger C., Sorensen O.W., and Ernst R.R. Two-dimensional correlation of connected NMR transitions. J. Am. Chem. Soc. 107 (1985) 6394-6396
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6394-6396
    • Griesinger, C.1    Sorensen, O.W.2    Ernst, R.R.3
  • 21
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 22
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., and Nicholls A. Classical electrostatics in biology and chemistry. Science 268 (1995) 1144-1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 26
    • 0029882204 scopus 로고    scopus 로고
    • Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy
    • Jung H., Windhaber R., Palm D., and Schnackerz K.D. Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy. Biochemistry 35 (1996) 6399-6405
    • (1996) Biochemistry , vol.35 , pp. 6399-6405
    • Jung, H.1    Windhaber, R.2    Palm, D.3    Schnackerz, K.D.4
  • 27
    • 2442456918 scopus 로고    scopus 로고
    • Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: an NMR study
    • Katragadda M., Maciejewski M.W., and Yeagle P.L. Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: an NMR study. Biochim. Biophys. Acta 1663 (2004) 74-81
    • (2004) Biochim. Biophys. Acta , vol.1663 , pp. 74-81
    • Katragadda, M.1    Maciejewski, M.W.2    Yeagle, P.L.3
  • 29
    • 0037008008 scopus 로고    scopus 로고
    • Evidence that helix 8 of rhodopsin acts as a membrane-dependent conformational switch
    • Krishna A.G., Menon S.T., Terry T.J., and Sakmar T.P. Evidence that helix 8 of rhodopsin acts as a membrane-dependent conformational switch. Biochemistry 41 (2002) 8298-8309
    • (2002) Biochemistry , vol.41 , pp. 8298-8309
    • Krishna, A.G.1    Menon, S.T.2    Terry, T.J.3    Sakmar, T.P.4
  • 30
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R.R., and Wuthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95 (1980) 1-6
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 31
    • 0025600997 scopus 로고
    • Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes
    • Lechleiter J., Hellmiss R., Duerson K., Ennulat D., David N., Clapham D., and Peralta E. Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes. EMBO J. 9 (1990) 4381-4390
    • (1990) EMBO J. , vol.9 , pp. 4381-4390
    • Lechleiter, J.1    Hellmiss, R.2    Duerson, K.3    Ennulat, D.4    David, N.5    Clapham, D.6    Peralta, E.7
  • 32
    • 0032558088 scopus 로고    scopus 로고
    • 10-helix contents of a helical peptide
    • 10-helix contents of a helical peptide. J. Am. Chem. Soc. 120 (1998) 7039-7048
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7039-7048
    • Long, H.W.1    Tycko, R.2
  • 33
    • 84915716471 scopus 로고
    • Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura S., and Ernst R. Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41 (1980) 95-117
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.2
  • 34
    • 49049150378 scopus 로고
    • Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclerar spins
    • Macura S., Huang Y., Suter D., and Ernst R.R. Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclerar spins. J. Magn. Reson. 43 (1981) 259-281
    • (1981) J. Magn. Reson. , vol.43 , pp. 259-281
    • Macura, S.1    Huang, Y.2    Suter, D.3    Ernst, R.R.4
  • 35
    • 0028921182 scopus 로고
    • Views of helical peptides: a proposal for the position of 3(10)-helix along the thermodynamic folding pathway
    • Millhauser G.L. Views of helical peptides: a proposal for the position of 3(10)-helix along the thermodynamic folding pathway. Biochemistry 34 (1995) 3873-3877
    • (1995) Biochemistry , vol.34 , pp. 3873-3877
    • Millhauser, G.L.1
  • 36
    • 0033574084 scopus 로고    scopus 로고
    • Regulation of Gi by the CB1 cannabinoid receptor C-terminal juxtamembrane region: structural requirements determined by peptide analysis
    • Mukhopadhyay S., Cowsik S.M., Lynn A.M., Welsh W.J., and Howlett A.C. Regulation of Gi by the CB1 cannabinoid receptor C-terminal juxtamembrane region: structural requirements determined by peptide analysis. Biochemistry 38 (1999) 3447-3455
    • (1999) Biochemistry , vol.38 , pp. 3447-3455
    • Mukhopadhyay, S.1    Cowsik, S.M.2    Lynn, A.M.3    Welsh, W.J.4    Howlett, A.C.5
  • 37
    • 0141733156 scopus 로고    scopus 로고
    • Rhodopsin determinants for transducin activation: a gain-of-function approach
    • Natochin M., Gasimov K.G., Moussaif M., and Artemyev N.O. Rhodopsin determinants for transducin activation: a gain-of-function approach. J. Biol. Chem. 278 (2003) 37574-37581
    • (2003) J. Biol. Chem. , vol.278 , pp. 37574-37581
    • Natochin, M.1    Gasimov, K.G.2    Moussaif, M.3    Artemyev, N.O.4
  • 38
    • 0037027953 scopus 로고    scopus 로고
    • Peptide conformational changes induced by tryptophan-phosphocholine interactions in a micelle
    • Neidigh J.W., and Andersen N.H. Peptide conformational changes induced by tryptophan-phosphocholine interactions in a micelle. Biopolymers 65 (2002) 354-361
    • (2002) Biopolymers , vol.65 , pp. 354-361
    • Neidigh, J.W.1    Andersen, N.H.2
  • 39
    • 0026630552 scopus 로고
    • Detection of G protein-activator regions in M4 subtype muscarinic, cholinergic, and alpha 2-adrenergic receptors based upon characteristics in primary structure
    • Okamoto T., and Nishimoto I. Detection of G protein-activator regions in M4 subtype muscarinic, cholinergic, and alpha 2-adrenergic receptors based upon characteristics in primary structure. J. Biol. Chem. 267 (1992) 8342-8346
    • (1992) J. Biol. Chem. , vol.267 , pp. 8342-8346
    • Okamoto, T.1    Nishimoto, I.2
  • 41
    • 0021764813 scopus 로고
    • Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure
    • Pardi A., Billeter M., and Wuthrich K. Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure. J. Mol. Biol. 180 (1984) 741-751
    • (1984) J. Mol. Biol. , vol.180 , pp. 741-751
    • Pardi, A.1    Billeter, M.2    Wuthrich, K.3
  • 42
    • 0027180807 scopus 로고
    • Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments
    • Rizo J., Blanco F.J., Kobe B., Bruch M.D., and Gierasch L.M. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry 32 (1993) 4881-4894
    • (1993) Biochemistry , vol.32 , pp. 4881-4894
    • Rizo, J.1    Blanco, F.J.2    Kobe, B.3    Bruch, M.D.4    Gierasch, L.M.5
  • 43
    • 0001350902 scopus 로고
    • Gradient-tailored water suppression for 1H-15N HSQC experiments optimized to retain full sensitivity
    • Sklenar V., Piotto M., Leppik R., and Saudek V. Gradient-tailored water suppression for 1H-15N HSQC experiments optimized to retain full sensitivity. J. Magn. Reson. 102 (1993) 241
    • (1993) J. Magn. Reson. , vol.102 , pp. 241
    • Sklenar, V.1    Piotto, M.2    Leppik, R.3    Saudek, V.4
  • 44
    • 0029978353 scopus 로고    scopus 로고
    • Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations
    • Smith L.J., Bolin K.A., Schwalbe H., MacArthur M.W., Thornton J.M., and Dobson C.M. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J. Mol. Biol. 255 (1996) 494-506
    • (1996) J. Mol. Biol. , vol.255 , pp. 494-506
    • Smith, L.J.1    Bolin, K.A.2    Schwalbe, H.3    MacArthur, M.W.4    Thornton, J.M.5    Dobson, C.M.6
  • 45
    • 0034826730 scopus 로고    scopus 로고
    • Alpha- and 3(10)-helix interconversion: a quantum-chemical study on polyalanine systems in the gas phase and in aqueous solvent
    • Topol I.A., Burt S.K., Deretey E., Tang T.H., Perczel A., Rashin A., and Csizmadia I.G. Alpha- and 3(10)-helix interconversion: a quantum-chemical study on polyalanine systems in the gas phase and in aqueous solvent. J. Am. Chem. Soc. 123 (2001) 6054-6060
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6054-6060
    • Topol, I.A.1    Burt, S.K.2    Deretey, E.3    Tang, T.H.4    Perczel, A.5    Rashin, A.6    Csizmadia, I.G.7
  • 46
    • 0032102452 scopus 로고    scopus 로고
    • Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles
    • Veeraraghavan S., Baleja J.D., and Gilbert G.E. Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles. Biochem. J. 332 (1998) 549-555
    • (1998) Biochem. J. , vol.332 , pp. 549-555
    • Veeraraghavan, S.1    Baleja, J.D.2    Gilbert, G.E.3
  • 47
    • 0032705301 scopus 로고    scopus 로고
    • G(i) activator region of alpha(2A)-adrenergic receptors: distinct basic residues mediate G(i) versus G(s) activation
    • Wade S.M., Lim W.K., Lan K.L., Chung D.A., Nanamori M., and Neubig R.R. G(i) activator region of alpha(2A)-adrenergic receptors: distinct basic residues mediate G(i) versus G(s) activation. Mol. Pharmacol. 56 (1999) 1005-1013
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1005-1013
    • Wade, S.M.1    Lim, W.K.2    Lan, K.L.3    Chung, D.A.4    Nanamori, M.5    Neubig, R.R.6
  • 48
    • 0026597879 scopus 로고
    • The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D.S., Sykes B.D., and Richards F.M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31 (1992) 1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 50
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wuthrich K., Billeter M., and Braun W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J. Mol. Biol. 180 (1984) 715-740
    • (1984) J. Mol. Biol. , vol.180 , pp. 715-740
    • Wuthrich, K.1    Billeter, M.2    Braun, W.3
  • 51
    • 13544267409 scopus 로고    scopus 로고
    • NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupled CB1 and CB2 receptors in membrane mimetic dodecylphosphocholine micelles
    • Xie X.Q., and Chen J.Z. NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupled CB1 and CB2 receptors in membrane mimetic dodecylphosphocholine micelles. J. Biol. Chem. 280 (2005) 3605-3612
    • (2005) J. Biol. Chem. , vol.280 , pp. 3605-3612
    • Xie, X.Q.1    Chen, J.Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.