메뉴 건너뛰기




Volumn 77, Issue 2, 2003, Pages 151-157

Picosecond Dynamics of a Peptide from the Acetylcholine Receptor Interacting with a Neurotoxin Probed by Tailored Tryptophan Fluorescence

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINERGIC RECEPTOR; COBROTOXIN; CYSTEINE; DEHYDRO N ACETYLTRYPTOPHANAMIDE; DISULFIDE; N,N DIMETHYLFORMAMIDE; NEUROTOXIN; PEPTIDE; SOLVENT; TRYPTOPHAN 2,3 DIOXYGENASE; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG; WATER; TRYPTOPHAN;

EID: 0038672775     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2003)077<0151:PDOAPF>2.0.CO;2     Document Type: Article
Times cited : (4)

References (34)
  • 2
    • 0035979711 scopus 로고    scopus 로고
    • Neuronal nicotinic receptors: From protein structure to function
    • Itier, V. and D. Bertrand (2001) Neuronal nicotinic receptors: from protein structure to function. FEBS Lett. 504, 118-125.
    • (2001) FEBS Lett. , vol.504 , pp. 118-125
    • Itier, V.1    Bertrand, D.2
  • 3
    • 0002315013 scopus 로고    scopus 로고
    • Structural model of nicotinic acetylcholine receptor isotypes bound to acetylcholine and nicotine
    • Schapira, M., R. Abagyan and M. Totrov (2002) Structural model of nicotinic acetylcholine receptor isotypes bound to acetylcholine and nicotine. BMC Struct. Biol. 2, 1.
    • (2002) BMC Struct. Biol. , vol.2 , pp. 1
    • Schapira, M.1    Abagyan, R.2    Totrov, M.3
  • 5
    • 0025753149 scopus 로고
    • Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand
    • Galzi, J. L., F. Revah, F. Bouet, A. Ménez, M. Goeldner, C. Hirth and J. P. Changeux (1991) Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand. Proc. Natl. Acad. Sci. USA 88, 5051-5055.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5051-5055
    • Galzi, J.L.1    Revah, F.2    Bouet, F.3    Ménez, A.4    Goeldner, M.5    Hirth, C.6    Changeux, J.P.7
  • 6
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. (1995) Acetylcholine receptor channel imaged in the open state. Nature 373, 37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 7
    • 0036304564 scopus 로고    scopus 로고
    • Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits
    • Unwin, N., A. Miyazawa, J. Li and Y. Fujiyoshi (2002) Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits. J. Mol. Biol. 319, 1165-1176.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1165-1176
    • Unwin, N.1    Miyazawa, A.2    Li, J.3    Fujiyoshi, Y.4
  • 8
    • 0022628717 scopus 로고
    • Kinetics of unliganded acetylcholine receptor channel gating
    • Jackson, M. B. (1986) Kinetics of unliganded acetylcholine receptor channel gating. Biophys. J. 49, 663-671.
    • (1986) Biophys. J. , vol.49 , pp. 663-671
    • Jackson, M.B.1
  • 9
    • 0019856889 scopus 로고
    • Fluctuations in the microsecond time range of the current through single acetylcholine receptor ion channels
    • Colquhoun, D. and B. Sakman (1981) Fluctuations in the microsecond time range of the current through single acetylcholine receptor ion channels. Nature 294, 464-466.
    • (1981) Nature , vol.294 , pp. 464-466
    • Colquhoun, D.1    Sakman, B.2
  • 10
    • 0020621092 scopus 로고
    • Multiple sites of action for noncompetitive blockers on acetylcholine receptor-rich membrane fragments from Torpedo marmorata
    • Heidmann, T., R. E. Oswald and J. P. Changeux (1983) Multiple sites of action for noncompetitive blockers on acetylcholine receptor-rich membrane fragments from Torpedo marmorata. Biochemistry 22, 3112-3127.
    • (1983) Biochemistry , vol.22 , pp. 3112-3127
    • Heidmann, T.1    Oswald, R.E.2    Changeux, J.P.3
  • 11
    • 0019800242 scopus 로고
    • Selective labeling of the delta subunit of the acetylcholine receptor by a covalent local anesthetic
    • Oswald, R. E. and J. P. Changeux (1981) Selective labeling of the delta subunit of the acetylcholine receptor by a covalent local anesthetic. Biochemistry 20, 7166-7174.
    • (1981) Biochemistry , vol.20 , pp. 7166-7174
    • Oswald, R.E.1    Changeux, J.P.2
  • 12
    • 0001607746 scopus 로고    scopus 로고
    • Snake neurotoxins that interact with nicotinic acetylcholine receptor
    • (Edited by E. J. Massaro). Humana Press Inc, Totowa, NJ
    • Servent, D. and A. Ménez (2001) Snake neurotoxins that interact with nicotinic acetylcholine receptor. In Handbook of Neurotoxicology, Vol. 1 (Edited by E. J. Massaro), pp. 385-425. Humana Press Inc, Totowa, NJ.
    • (2001) Handbook of Neurotoxicology , vol.1 , pp. 385-425
    • Servent, D.1    Ménez, A.2
  • 13
    • 0035933887 scopus 로고    scopus 로고
    • The solution structure of the complex formed between α -bungarotoxin and an 18-mer cognate peptide derived from the α-subunit of the nicotinic acetylcholine receptor from Torpedo californica
    • Zeng, H., L. Moise, M. A. Grant and E. Hawrot (2001) The solution structure of the complex formed between α-bungarotoxin and an 18-mer cognate peptide derived from the α-subunit of the nicotinic acetylcholine receptor from Torpedo californica. J. Biol. Chem. 276, 22930-22940.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22930-22940
    • Zeng, H.1    Moise, L.2    Grant, M.A.3    Hawrot, E.4
  • 14
    • 0035826660 scopus 로고    scopus 로고
    • NMR mapping and secondary structure determination of the major acetylcholine receptor α-subunit determinant interacting with α-bungarotoxin
    • Samson, A. O., J. H. Chill, E. Rodriguez, T. Scherf and J. Anglister (2001) NMR mapping and secondary structure determination of the major acetylcholine receptor α-subunit determinant interacting with α-bungarotoxin. Biochemistry 40, 5464-5473.
    • (2001) Biochemistry , vol.40 , pp. 5464-5473
    • Samson, A.O.1    Chill, J.H.2    Rodriguez, E.3    Scherf, T.4    Anglister, J.5
  • 15
    • 0027371744 scopus 로고
    • NMR solution structure of an α-bungarotoxin/nicotinic receptor peptide complex
    • Basus, V. J., G. Song and E. Hawrot (1993) NMR solution structure of an α-bungarotoxin/nicotinic receptor peptide complex. Biochemistry 32, 12290-12298.
    • (1993) Biochemistry , vol.32 , pp. 12290-12298
    • Basus, V.J.1    Song, G.2    Hawrot, E.3
  • 16
    • 0028125739 scopus 로고
    • Interaction of protein ligands with receptor fragments. On the residues of curaremimetic toxins that recognize fragments 128-142 and 185-199 of the α-subunit of the nicotinic acetylcholine receptor
    • Fulachier, M. H., G. Mourier, J. Cotton, D. Servent and A. Ménez (1994) Interaction of protein ligands with receptor fragments. On the residues of curaremimetic toxins that recognize fragments 128-142 and 185-199 of the α-subunit of the nicotinic acetylcholine receptor. FEBS Lett. 338, 331-338.
    • (1994) FEBS Lett. , vol.338 , pp. 331-338
    • Fulachier, M.H.1    Mourier, G.2    Cotton, J.3    Servent, D.4    Ménez, A.5
  • 18
    • 0028849457 scopus 로고
    • Using 7-azatryptophan to probe small molecule-protein interactions on the picosecond time scale: The complex of avidin and biotinylated 7-azatryptophan
    • Rich, R. L., F. Gai, J. W. Lane, J. W. Petrich and A. W. Schwabacher (1995) Using 7-azatryptophan to probe small molecule-protein interactions on the picosecond time scale: the complex of avidin and biotinylated 7-azatryptophan. J. Am. Chem. Soc. 117, 733-739.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 733-739
    • Rich, R.L.1    Gai, F.2    Lane, J.W.3    Petrich, J.W.4    Schwabacher, A.W.5
  • 19
    • 0033227998 scopus 로고    scopus 로고
    • Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan
    • Das, K., K. D. Ashby, A. V. Smirnov, F. C. Reinach, J. W. Petrich and C. S. Farah (1999) Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan. Photochem. Photobiol. 70, 719-730.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 719-730
    • Das, K.1    Ashby, K.D.2    Smirnov, A.V.3    Reinach, F.C.4    Petrich, J.W.5    Farah, C.S.6
  • 20
    • 0032554618 scopus 로고    scopus 로고
    • Internal motion of lysozyme studied by time-resolved fluorescence depolarization of tryptophan residues
    • Nishimoto, E., S. Yamashita, A. G. Szabo and T. Imoto (1998) Internal motion of lysozyme studied by time-resolved fluorescence depolarization of tryptophan residues. Biochemistry 37, 5599-5607.
    • (1998) Biochemistry , vol.37 , pp. 5599-5607
    • Nishimoto, E.1    Yamashita, S.2    Szabo, A.G.3    Imoto, T.4
  • 21
    • 0037183078 scopus 로고    scopus 로고
    • Dynamics of 7-azatryptophan derivatives in micellar media. Elucidating the interactions between peptide oligomers and micelles
    • Kelepouris, L. and G. J. Blanchard (2002) Dynamics of 7-azatryptophan derivatives in micellar media. Elucidating the interactions between peptide oligomers and micelles. J. Phys. Chem. B 106, 6600-6608.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6600-6608
    • Kelepouris, L.1    Blanchard, G.J.2
  • 22
    • 0021262475 scopus 로고
    • Enzymatic dehydrogenation of tryptophan residues of human globins by tryptophan side chain oxidase II
    • Takai, K., Y. Sasai, H. Morimoto, H. Yamazaki, H. Yoshii and S. Inoue (1984) Enzymatic dehydrogenation of tryptophan residues of human globins by tryptophan side chain oxidase II. J. Biol. Chem. 259, 4452-4457.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4452-4457
    • Takai, K.1    Sasai, Y.2    Morimoto, H.3    Yamazaki, H.4    Yoshii, H.5    Inoue, S.6
  • 23
    • 0028338565 scopus 로고
    • Purification and partial characterization of an amino acid α,β-dehydrogenase. L-tryptophan 2′,3′-oxidase from Chromobacterium violaceum
    • Genet, R., C. Denoyelle and A. Ménez (1994) Purification and partial characterization of an amino acid α,β-dehydrogenase, L-tryptophan 2′,3′-oxidase from Chromobacterium violaceum. J. Biol. Chem. 269, 18177-18184.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18177-18184
    • Genet, R.1    Denoyelle, C.2    Ménez, A.3
  • 24
    • 0028970608 scopus 로고
    • L-Tryptophan 2′,3′-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications
    • Genet, R., P. H. Bénetti, A. Hammadi and A. Ménez (1995) L-Tryptophan 2′,3′-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications. J. Biol. Chem. 270, 23540-23545.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23540-23545
    • Genet, R.1    Bénetti, P.H.2    Hammadi, A.3    Ménez, A.4
  • 25
    • 0034013918 scopus 로고    scopus 로고
    • Chemical engineering of a three-fingered toxin with anti-α7 neuronal acetylcholine receptor activity
    • Mourier, G., D. Servent, S. Zinn-Justin and A. Ménez (2000) Chemical engineering of a three-fingered toxin with anti-α7 neuronal acetylcholine receptor activity. Protein Eng. 13, 217-225.
    • (2000) Protein Eng. , vol.13 , pp. 217-225
    • Mourier, G.1    Servent, D.2    Zinn-Justin, S.3    Ménez, A.4
  • 26
    • 0000352971 scopus 로고
    • Steady-state and time-resolved fluorescence anisotropy of 7-azaindole and its derivatives
    • Rich, R. L., Y. Chen, D. Neven, M. Négrerie, F. Gai and J. W. Petrich (1993) Steady-state and time-resolved fluorescence anisotropy of 7-azaindole and its derivatives. J. Phys. Chem. 97, 1781-1788.
    • (1993) J. Phys. Chem. , vol.97 , pp. 1781-1788
    • Rich, R.L.1    Chen, Y.2    Neven, D.3    Négrerie, M.4    Gai, F.5    Petrich, J.W.6
  • 28
    • 0020763601 scopus 로고
    • On the origin of nonexponential fluorescence decay in tryptophan and its derivatives
    • Petrich, J. W., M. C. Chang, D. B. McDonald and G. R. Fleming (1983) On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. J. Am. Chem. Soc. 105, 3824-3832.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3824-3832
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.B.3    Fleming, G.R.4
  • 29
    • 0028331766 scopus 로고
    • Dynamics of the active loop of snake toxins as probed by time-resolved polarized tryptophan fluorescence
    • Blandin, P., F. Mérola, J. C. Brochon, O. Trémeau and A. Ménez (1994) Dynamics of the active loop of snake toxins as probed by time-resolved polarized tryptophan fluorescence. Biochemistry 33, 2610-2619.
    • (1994) Biochemistry , vol.33 , pp. 2610-2619
    • Blandin, P.1    Mérola, F.2    Brochon, J.C.3    Trémeau, O.4    Ménez, A.5
  • 31
    • 17144439412 scopus 로고    scopus 로고
    • E/Z-configurational assignment of N-acetyl-α,β -dehydrotryptophan ethyl ester produced by L-tryptophan 2′,3′ -oxidase from Chromobacterium violaceum
    • Hammadi, A., A. Ménez and R. Genet (1996) E/Z-configurational assignment of N-acetyl-α,β-dehydrotryptophan ethyl ester produced by L-tryptophan 2′,3′-oxidase from Chromobacterium violaceum. Tetrahedron Lett. 37, 3309-3312.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 3309-3312
    • Hammadi, A.1    Ménez, A.2    Genet, R.3
  • 32
    • 0026472379 scopus 로고
    • Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: A proton NMR and molecular modeling study
    • Zinn-Justin, S., C. Roumestand, B. Gilquin, F. Bontems, A. Ménez and F. Toma (1992) Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study. Biochemistry 31, 11335-11347.
    • (1992) Biochemistry , vol.31 , pp. 11335-11347
    • Zinn-Justin, S.1    Roumestand, C.2    Gilquin, B.3    Bontems, F.4    Ménez, A.5    Toma, F.6
  • 33
    • 0037889340 scopus 로고
    • Picosecond fluorescence studies of polypeptide dynamics: Fluorescence anisotropies and lifetimes
    • Chen, L. X., J. W. Petrich, G. R. Fleming and A. Perico (1987) Picosecond fluorescence studies of polypeptide dynamics: fluorescence anisotropies and lifetimes. Chem. Phys. Lett. 139, 55-61.
    • (1987) Chem. Phys. Lett. , vol.139 , pp. 55-61
    • Chen, L.X.1    Petrich, J.W.2    Fleming, G.R.3    Perico, A.4
  • 34
    • 0037130458 scopus 로고    scopus 로고
    • The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR
    • Samson, A. O., T. Scherf, M. Eisenstein, J. H. Chill and J. Anglister (2002) The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR. Neuron 35, 319-332.
    • (2002) Neuron , vol.35 , pp. 319-332
    • Samson, A.O.1    Scherf, T.2    Eisenstein, M.3    Chill, J.H.4    Anglister, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.