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Volumn 1699, Issue 1-2, 2004, Pages 77-86

Circular dichroism and fluorescence of a tyrosine side-chain residue monitors the concentration-dependent equilibrium between U-shaped and coiled-coil conformations of a peptide derived from the catalytic core of HIV-1 integrase

Author keywords

Amphipathic helix; ANS; Circular dichroism; Coiled coil; Concentration dependence; Fluorescence enhancement, quenching and temperature coefficient; Side chain as chromophore and fluorophore; Stern Volmer; Trifluoroethanol

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; INTEGRASE; PEPTIDE DERIVATIVE; TRIFLUOROETHANOL; TYROSINE; VIRUS ENZYME;

EID: 2542452872     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(04)00024-X     Document Type: Article
Times cited : (6)

References (53)
  • 1
    • 0004131381 scopus 로고    scopus 로고
    • J.M. Coffin, S.H. Hugghes, & H.E. Varmus. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Brown P.O. Coffin J.M., Hugghes S.H., Varmus H.E. Retroviruses. 1997;161-203 Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • (1997) Retroviruses , pp. 161-203
    • Brown, P.O.1
  • 2
    • 0031434606 scopus 로고    scopus 로고
    • Molecular mechanisms in retrovirus DNA integration
    • Asante-Appiah E., Skalka A.M. Molecular mechanisms in retrovirus DNA integration. Antivir. Res. 36:1997;139-156
    • (1997) Antivir. Res. , vol.36 , pp. 139-156
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 6
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro
    • Engelman A., Craigie R. Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro. J. Virol. 66:1992;6361-6369
    • (1992) J. Virol. , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 7
    • 0027179694 scopus 로고
    • Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex
    • Engelman A., Bushman F.D., Craigie R. Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBO J. 12:1993;3269-3275
    • (1993) EMBO J. , vol.12 , pp. 3269-3275
    • Engelman, A.1    Bushman, F.D.2    Craigie, R.3
  • 8
    • 0027246609 scopus 로고
    • Complementation between HIV integrase proteins mutated in different domains
    • van Gent D.C., Vink C., Groeneger A.A., Plasterk R.H. Complementation between HIV integrase proteins mutated in different domains. EMBO J. 12:1993;3261-3267
    • (1993) EMBO J. , vol.12 , pp. 3261-3267
    • Van Gent, D.C.1    Vink, C.2    Groeneger, A.A.3    Plasterk, R.H.4
  • 9
    • 0032617443 scopus 로고    scopus 로고
    • K. Maramorosh, F.A. Murphy, Shatkin A.J. San Diego: Academic Press
    • Wlodawer A. Maramorosh K., Murphy F.A., Shatkin A.J. Advances in Virus Research. vol. 52:1999;335-350 Academic Press, San Diego
    • (1999) Advances in Virus Research , vol.52 , pp. 335-350
    • Wlodawer, A.1
  • 17
    • 0032601402 scopus 로고    scopus 로고
    • K. Maramorosh, F.A. Murphy, Shatkin A.J. San Diego: Academic Press
    • Esposito D., Craigie R. Maramorosh K., Murphy F.A., Shatkin A.J. Advances in Virus Research. vol. 52:1999;319-333 Academic Press, San Diego
    • (1999) Advances in Virus Research , vol.52 , pp. 319-333
    • Esposito, D.1    Craigie, R.2
  • 18
    • 0032510707 scopus 로고    scopus 로고
    • Photo-cross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type-1 integrase-DNA complex
    • Heuer T.S., Brown P.O. Photo-cross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type-1 integrase-DNA complex. Biochemistry. 37:1998;6667-6678
    • (1998) Biochemistry , vol.37 , pp. 6667-6678
    • Heuer, T.S.1    Brown, P.O.2
  • 19
    • 0035796559 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase: Arrangement of protein domains in active cDNA complexes
    • Gao K., Buttler S.L., Bushman F. Human immunodeficiency virus type 1 integrase: arrangement of protein domains in active cDNA complexes. EMBO J. 20:2001;3565-3576
    • (2001) EMBO J. , vol.20 , pp. 3565-3576
    • Gao, K.1    Buttler, S.L.2    Bushman, F.3
  • 20
    • 0037234457 scopus 로고    scopus 로고
    • Modeling HIV-1 integrase complexes based on their hydrodynamic properties
    • Podtelezhnikov A.A., Gao K., Bushman F.D., McCammon J.A. Modeling HIV-1 integrase complexes based on their hydrodynamic properties. Biopolymers. 68:2003;110-120
    • (2003) Biopolymers , vol.68 , pp. 110-120
    • Podtelezhnikov, A.A.1    Gao, K.2    Bushman, F.D.3    McCammon, J.A.4
  • 22
    • 0034681278 scopus 로고    scopus 로고
    • X-ray structure of simian immunodeficiency virus integrase containing the core and C-terminal domain (residues 50-293) - An initial glance of the viral DNA binding platform
    • Chen Z., Yan Y., Munshi S., Li Y., Zugay-Murphy J., Xu B., Witmer M., Felock P., Wolfe A., Sardana V., Emini E.A., Hazuda D., Kuo L.C. X-ray structure of simian immunodeficiency virus integrase containing the core and C-terminal domain (residues 50-293) - an initial glance of the viral DNA binding platform. J. Mol. Biol. 296:2000;521-533
    • (2000) J. Mol. Biol. , vol.296 , pp. 521-533
    • Chen, Z.1    Yan, Y.2    Munshi, S.3    Li, Y.4    Zugay-Murphy, J.5    Xu, B.6    Witmer, M.7    Felock, P.8    Wolfe, A.9    Sardana, V.10    Emini, E.A.11    Hazuda, D.12    Kuo, L.C.13
  • 23
    • 0037126629 scopus 로고    scopus 로고
    • Structure of a two-domain fragment of HIV-1 integrase: Implications for domain organization in the intact protein
    • Wang J.Y., Ling H., Yang W., Craigie R. Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein. EMBO J. 20:2001;7333-7343
    • (2001) EMBO J. , vol.20 , pp. 7333-7343
    • Wang, J.Y.1    Ling, H.2    Yang, W.3    Craigie, R.4
  • 25
    • 0006611422 scopus 로고    scopus 로고
    • A synthetic peptide from the human immunodeficiency virus type-1 integrase exhibits coiled-coil properties and interferes with the in vivo integration activity of the enzyme. Correlated biochemical and spectroscopic results
    • Sourgen F., Maroun R.G., Frère V., Bouziane M., Auclair C., Troalen F., Fermandjian S. A synthetic peptide from the human immunodeficiency virus type-1 integrase exhibits coiled-coil properties and interferes with the in vivo integration activity of the enzyme. Correlated biochemical and spectroscopic results. Eur. J. Biochem. 260:1996;145-155
    • (1996) Eur. J. Biochem. , vol.260 , pp. 145-155
    • Sourgen, F.1    Maroun, R.G.2    Frère, V.3    Bouziane, M.4    Auclair, C.5    Troalen, F.6    Fermandjian, S.7
  • 26
    • 0033557819 scopus 로고    scopus 로고
    • Conformational aspects of HIV-1 integrase inhibition by a peptide derived from the enzyme central domain and by antibodies raised against this peptide
    • Maroun R.G., Krebs D., Roshani M., Porumb H., Auclair C., Troalen F., Fermandjian S. Conformational aspects of HIV-1 integrase inhibition by a peptide derived from the enzyme central domain and by antibodies raised against this peptide. Eur. J. Biochem. 260:1999;145-155
    • (1999) Eur. J. Biochem. , vol.260 , pp. 145-155
    • Maroun, R.G.1    Krebs, D.2    Roshani, M.3    Porumb, H.4    Auclair, C.5    Troalen, F.6    Fermandjian, S.7
  • 31
    • 0032054082 scopus 로고    scopus 로고
    • Helical and coiled-coil forming properties of peptides derived from and inhibiting human immunodeficiency virus type 1 integrase assessed by 1H-NMR. Use of NH temperature coefficients to probe coiled-coil structures
    • Krebs D., Maroun R.G., Sourgen F., Troalen F., Davoust D., Fermandjian S. Helical and coiled-coil forming properties of peptides derived from and inhibiting human immunodeficiency virus type 1 integrase assessed by 1H-NMR. Use of NH temperature coefficients to probe coiled-coil structures. Eur. J. Biochem. 253:1998;236-244
    • (1998) Eur. J. Biochem. , vol.253 , pp. 236-244
    • Krebs, D.1    Maroun, R.G.2    Sourgen, F.3    Troalen, F.4    Davoust, D.5    Fermandjian, S.6
  • 32
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled coil structures
    • Lupas A. Prediction and analysis of coiled coil structures. Methods Enzymol. 266:1996;513-525
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 33
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/ water mixtures back to water
    • Luo P., Baldwin R.L. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry. 36:1997;8413-8421
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 34
    • 0030567341 scopus 로고    scopus 로고
    • Mechanisms of stabilization of helical conformations of polypeptides by water containing trifluoroethanol
    • Cammers-Goodwin A., Allen T.J., Oslick S.L., McClure K.F., Lee J.H., Kemp D.S. Mechanisms of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J. Am. Chem. Soc. 118:1996;3082-3090
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3082-3090
    • Cammers-Goodwin, A.1    Allen, T.J.2    Oslick, S.L.3    McClure, K.F.4    Lee, J.H.5    Kemp, D.S.6
  • 35
    • 0033607791 scopus 로고    scopus 로고
    • Self-association and domains of interactions of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by analytical ultracentrifugation and NMR experiments in trifluoroethanol/H(2)O mixtures
    • Maroun R.G., Krebs D., El Antri S., Deroussent A., Lescot E., Troalen F., Porumb H., Goldberg M.E., Fermandjian S. Self-association and domains of interactions of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by analytical ultracentrifugation and NMR experiments in trifluoroethanol/H(2)O mixtures. J. Biol. Chem. 274:1999;34174-34185
    • (1999) J. Biol. Chem. , vol.274 , pp. 34174-34185
    • Maroun, R.G.1    Krebs, D.2    El Antri, S.3    Deroussent, A.4    Lescot, E.5    Troalen, F.6    Porumb, H.7    Goldberg, M.E.8    Fermandjian, S.9
  • 36
    • 0037442549 scopus 로고    scopus 로고
    • Structural changes and facilitated association of tropoelastin
    • Muiznieks L.D., Jensen S.A., Weiss A.S. Structural changes and facilitated association of tropoelastin. Arch. Biochem. Biophys. 410:2003;317-323
    • (2003) Arch. Biochem. Biophys. , vol.410 , pp. 317-323
    • Muiznieks, L.D.1    Jensen, S.A.2    Weiss, A.S.3
  • 37
    • 0036112239 scopus 로고    scopus 로고
    • Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel
    • Ohlenschlager O., Hojo H., Ramachandran R., Gorlach M., Haris P.I. Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel. Biophys. J. 82:2002;2995-3002
    • (2002) Biophys. J. , vol.82 , pp. 2995-3002
    • Ohlenschlager, O.1    Hojo, H.2    Ramachandran, R.3    Gorlach, M.4    Haris, P.I.5
  • 39
    • 0037062632 scopus 로고    scopus 로고
    • Distinct structural elements that direct solution aggregation and membrane assembly in the channel-forming peptide M2GlyR
    • Broughman J.R., Shank L.P., Takeguchi W., Schultz B.D., Iwamoto T., Mitchell K.E., Tomich J.M. Distinct structural elements that direct solution aggregation and membrane assembly in the channel-forming peptide M2GlyR. Biochemistry. 41:2002;7350-7358
    • (2002) Biochemistry , vol.41 , pp. 7350-7358
    • Broughman, J.R.1    Shank, L.P.2    Takeguchi, W.3    Schultz, B.D.4    Iwamoto, T.5    Mitchell, K.E.6    Tomich, J.M.7
  • 40
    • 0037472804 scopus 로고    scopus 로고
    • Comparison of proto-oncogenic and mutant forms of the transmembrane region of the Neu receptor in TFE
    • Houliston R.S., Hodges R.S., Sharom F.J., Davis J.H. Comparison of proto-oncogenic and mutant forms of the transmembrane region of the Neu receptor in TFE. FEBS Lett. 535:2003;39-43
    • (2003) FEBS Lett. , vol.535 , pp. 39-43
    • Houliston, R.S.1    Hodges, R.S.2    Sharom, F.J.3    Davis, J.H.4
  • 41
    • 0037026868 scopus 로고    scopus 로고
    • Trifluoroethanol and binding to model membranes stabilize a predicted turn in a peptide corresponding to the first extracellular loop of the angiotensin II AT(1A) receptor
    • Salinas R.K., Shida C.S., Pertinhez T.A., Spisni A., Nakaie C.R., Paiva A.C., Schreier S. Trifluoroethanol and binding to model membranes stabilize a predicted turn in a peptide corresponding to the first extracellular loop of the angiotensin II AT(1A) receptor. Biopolymers. 65:2002;21-31
    • (2002) Biopolymers , vol.65 , pp. 21-31
    • Salinas, R.K.1    Shida, C.S.2    Pertinhez, T.A.3    Spisni, A.4    Nakaie, C.R.5    Paiva, A.C.6    Schreier, S.7
  • 42
    • 0037378766 scopus 로고    scopus 로고
    • Polyproline Type II Conformation in the C-Terminal Domain of the Nuclear Pore Complex Protein gp210
    • Pilpel Y., Bogin O., Brumfeld V., Reich Z. Polyproline Type II Conformation in the C-Terminal Domain of the Nuclear Pore Complex Protein gp210. Biochemistry. 42:2003;3519-3526
    • (2003) Biochemistry , vol.42 , pp. 3519-3526
    • Pilpel, Y.1    Bogin, O.2    Brumfeld, V.3    Reich, Z.4
  • 43
    • 0037442557 scopus 로고    scopus 로고
    • Identification and solution conformation of multiple epitopes recognized by a MUC2 mucin-specific monoclonal antibody
    • Uray K., Price M.R., Majer Z., Vass E., Hollosi M., Hudecz F. Identification and solution conformation of multiple epitopes recognized by a MUC2 mucin-specific monoclonal antibody. Arch. Biochem. Biophys. 410:2003;254-260
    • (2003) Arch. Biochem. Biophys. , vol.410 , pp. 254-260
    • Uray, K.1    Price, M.R.2    Majer, Z.3    Vass, E.4    Hollosi, M.5    Hudecz, F.6
  • 45
    • 0038043276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all beta-barrel protein-partially structured intermediate state(s) is a precursor for fibril formation
    • Srisailam S., Kumar T.K., Rajalingam D., Kathir K.M., Sheu H.S., Jan F.J., Chao P.C., Yu C. Amyloid-like fibril formation in an all beta-barrel protein-partially structured intermediate state(s) is a precursor for fibril formation. J. Biol. Chem. 278:2003;17701-17709
    • (2003) J. Biol. Chem. , vol.278 , pp. 17701-17709
    • Srisailam, S.1    Kumar, T.K.2    Rajalingam, D.3    Kathir, K.M.4    Sheu, H.S.5    Jan, F.J.6    Chao, P.C.7    Yu, C.8
  • 46
    • 0037047321 scopus 로고    scopus 로고
    • NMR structure and dynamics of a receptor-active apolipoprotein e peptide
    • Raussens V., Slupsky C.M., Ryan R.O., Sykes B.D. NMR structure and dynamics of a receptor-active apolipoprotein E peptide. J. Biol. Chem. 277:2002;29172-29180
    • (2002) J. Biol. Chem. , vol.277 , pp. 29172-29180
    • Raussens, V.1    Slupsky, C.M.2    Ryan, R.O.3    Sykes, B.D.4
  • 47
    • 0033528673 scopus 로고    scopus 로고
    • Amphipatic α-helix bundle organization of lipid-free chicken apolipoprotein A-I
    • Kiss R.S., Kay C.M., Ryan R.O. Amphipatic α-helix bundle organization of lipid-free chicken apolipoprotein A-I. Biochemistry. 38:1999;4327-4334
    • (1999) Biochemistry , vol.38 , pp. 4327-4334
    • Kiss, R.S.1    Kay, C.M.2    Ryan, R.O.3
  • 48
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. the quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry. 10:1971;3254-3263
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 49
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink M.R., Ghiron C.A. Fluorescence quenching studies with proteins. Anal. Biochem. 114:1981;199-227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 50
    • 0025689272 scopus 로고
    • The effect of conformation on the CD of interacting helices: A theoretical study of tropomyosin
    • Cooper T.M., Woody R.W. The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosin. Biopolymers. 30:1990;657-676
    • (1990) Biopolymers , vol.30 , pp. 657-676
    • Cooper, T.M.1    Woody, R.W.2
  • 51
    • 0029884694 scopus 로고    scopus 로고
    • GOR secondary structure prediction method version IV
    • Garnier J., Gibrat J.-F., Robson B. GOR secondary structure prediction method version IV. Methods Enzymol. 266:1996;540-553
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.-F.2    Robson, B.3
  • 52
    • 0030152789 scopus 로고    scopus 로고
    • Tyrosines in two-stranded coiled coils are CD active near 280 nm even in the absence of interhelix tyrosine-tyrosine interactions
    • Holtzer M.E., Adams K., Lovett E.G., Holtzer A. Tyrosines in two-stranded coiled coils are CD active near 280 nm even in the absence of interhelix tyrosine-tyrosine interactions. Biopolymers. 38:1996;669-671
    • (1996) Biopolymers , vol.38 , pp. 669-671
    • Holtzer, M.E.1    Adams, K.2    Lovett, E.G.3    Holtzer, A.4


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