메뉴 건너뛰기




Volumn 13, Issue 4, 2007, Pages 281-290

Monitoring conformational changes in protein complexes using chemical cross-linking and Fourier transform ion cyclotron resonance mass spectrometry: The effect of calcium binding on the calmodulin-melittin complex

Author keywords

Calmodulin; Chemical cross linking; FT ICR mass spectrometry; Melittin; Protein complex; Protein conformation

Indexed keywords

1 ETHYL 3 (3 (DIETHYLAMINO)PROPYL)CARBODIIMIDE; 1-ETHYL-3-(3-(DIETHYLAMINO)PROPYL)CARBODIIMIDE; CALCIUM; CALMODULIN; CROSS LINKING REAGENT; CYANAMIDE; MELITTIN; SUBERIC ACID BIS(N HYDROXYSUCCINIMIDE) ESTER; SUCCINIMIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 36348970617     PISSN: 14690667     EISSN: None     Source Type: Journal    
DOI: 10.1255/ejms.882     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 0017338248 scopus 로고
    • Chemical cross-linking-reagents and problems in studies of membrane structure
    • doi: 10.1146/annurev.bi.46.070177.002515
    • K. Peters and F.M. Richards, "Chemical cross-linking-reagents and problems in studies of membrane structure", Ann. Rev. Biochem. 46, 523-551 (1977). doi: 10.1146/annurev.bi.46.070177.002515
    • (1977) Ann. Rev. Biochem , vol.46 , pp. 523-551
    • Peters, K.1    Richards, F.M.2
  • 2
    • 0027203297 scopus 로고
    • New photolabelling and cross-linking methods
    • doi: 10.1146/annurev.bi.62. 070193.002411
    • J. Brunner, "New photolabelling and cross-linking methods", Ann. Rev. Biochem. 62, 483-514 (1993). doi: 10.1146/annurev.bi.62. 070193.002411
    • (1993) Ann. Rev. Biochem , vol.62 , pp. 483-514
    • Brunner, J.1
  • 3
    • 0033970146 scopus 로고    scopus 로고
    • Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques
    • doi: 10.1016/S1367-5931(99)00047-2
    • D.A. Fancy, "Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques", Curr. Opin. Chem. Biol. 4, 28-33 (2000). doi: 10.1016/S1367-5931(99)00047-2
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 28-33
    • Fancy, D.A.1
  • 4
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • doi: 10.1073/pnas.090099097
    • M.M. Young, N. Tang, J.C. Hempel, C.M. Oshiro, E.W. Taylor, I.D. Kuntz, B.W. Gibson and G. Dollinger, "High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry", Proc. Nat. Acad. Sci. USA 97, 5802-5806 (2000). doi: 10.1073/pnas.090099097
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 5802-5806
    • Young, M.M.1    Tang, N.2    Hempel, J.C.3    Oshiro, C.M.4    Taylor, E.W.5    Kuntz, I.D.6    Gibson, B.W.7    Dollinger, G.8
  • 5
    • 0023831887 scopus 로고
    • Interactive properties of calmodulin
    • J.A Cox, "Interactive properties of calmodulin", Biochem. J. 249, 621-629 (1988).
    • (1988) Biochem. J , vol.249 , pp. 621-629
    • Cox, J.A.1
  • 6
    • 0028506122 scopus 로고
    • Calmodulin - A versatile calcium mediator protein
    • H.J. Vogel, "Calmodulin - A versatile calcium mediator protein", Biochem. Cell Biol. 72, 357-376 (1994).
    • (1994) Biochem. Cell Biol , vol.72 , pp. 357-376
    • Vogel, H.J.1
  • 8
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2Å resolution
    • doi: 10.1016/0022-2836(88)90608-0
    • Y.S. Babu, C.E. Bugg and W.J. Cook, "Structure of calmodulin refined at 2.2Å resolution", J. Mol. Biol. 204, 191-204 (1988). doi: 10.1016/0022-2836(88)90608-0
    • (1988) J. Mol. Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 9
    • 0027052523 scopus 로고
    • Calmodulin structure refined at 1.7 A resolution
    • doi: 10.1016/0022-2836(92)90324-0
    • R. Chattopadhyaya, W.E. Meador, A.R. Means and P.A. Quiocho, "Calmodulin structure refined at 1.7 A resolution", J. Mol. Biol. 228, 1117-1192 (1992). doi: 10.1016/0022-2836(92)90324-0
    • (1992) J. Mol. Biol , vol.228 , pp. 1117-1192
    • Chattopadhyaya, R.1    Meador, W.E.2    Means, A.R.3    Quiocho, P.A.4
  • 10
    • 0024279165 scopus 로고
    • The central helix of calmodulin functions as a flexible tether
    • A. Persechini and R.H. Kretsinger, "The central helix of calmodulin functions as a flexible tether", J. Biol. Chem. 263, 12175-12178 (1988).
    • (1988) J. Biol. Chem , vol.263 , pp. 12175-12178
    • Persechini, A.1    Kretsinger, R.H.2
  • 11
    • 0027945446 scopus 로고
    • Molecular tuning of ion-binding to calcium signalling
    • J.J. Falke, S.K. Drake, A.L. Hazard and O. Peersen, "Molecular tuning of ion-binding to calcium signalling", Q. Rev. Biophys. 27, 219-290 (1994).
    • (1994) Q. Rev. Biophys , vol.27 , pp. 219-290
    • Falke, J.J.1    Drake, S.K.2    Hazard, A.L.3    Peersen, O.4
  • 12
    • 0025996973 scopus 로고
    • Secondary structure and side-chain H-1 and C-13 resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR-spectroscopy
    • doi: 10.1021/bi00102a013
    • M. Ikura, S. Pera, G. Barbato, L.E. Kay, M. Krinks,and A. Bax, "Secondary structure and side-chain H-1 and C-13 resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR-spectroscopy", Biochemistry 30, 9216-9228 (1991). doi: 10.1021/bi00102a013
    • (1991) Biochemistry , vol.30 , pp. 9216-9228
    • Ikura, M.1    Pera, S.2    Barbato, G.3    Kay, L.E.4    Krinks, M.5    Bax, A.6
  • 13
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • doi: 10.1126/science.1585175
    • M. Ikura, M. Clore, A.M. Gronenborn, G. Zhu, C.B Klee and A. Bax, "Solution structure of a calmodulin-target peptide complex by multidimensional NMR", Science 256, 632-638 (1992). doi: 10.1126/science.1585175
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 14
    • 0033514432 scopus 로고    scopus 로고
    • Calcium-dependent and -independent interactions of the calmodulin-binding domain of cyclic nucleotide phosphodiesterase with calmodulin
    • doi: 10.1021/bi9816453
    • T. Yuan, M.P. Walsh, C. Sutherland, H. Fabian and H.J. Vogel, "Calcium-dependent and -independent interactions of the calmodulin-binding domain of cyclic nucleotide phosphodiesterase with calmodulin", Biochemistry 38, 1446-1455 (1999). doi: 10.1021/bi9816453
    • (1999) Biochemistry , vol.38 , pp. 1446-1455
    • Yuan, T.1    Walsh, M.P.2    Sutherland, C.3    Fabian, H.4    Vogel, H.J.5
  • 16
    • 0026662333 scopus 로고
    • Use of engineered proteins with internal tryptophan reporter groups and perturbation techniques to probe the mechanism of ligand protein interactions-Investigation of the mechanism of calcium-binding to calmodulin
    • doi: 10.1021/bi00149a046
    • M.C. Kilhoffer, F. Kubina, F. Travers and J. Haiech, "Use of engineered proteins with internal tryptophan reporter groups and perturbation techniques to probe the mechanism of ligand protein interactions-Investigation of the mechanism of calcium-binding to calmodulin", Biochemistry 31, 8098-8106 (1992). doi: 10.1021/bi00149a046
    • (1992) Biochemistry , vol.31 , pp. 8098-8106
    • Kilhoffer, M.C.1    Kubina, F.2    Travers, F.3    Haiech, J.4
  • 17
    • 0028804927 scopus 로고
    • Cooperativity -over-the-hill
    • doi: 10.1016/S0968- 0004(00)89115-X
    • S. Forsen and S. Linse, "Cooperativity -over-the-hill", Trends Biochem. Sci. 20, 495-497 (1995). doi: 10.1016/S0968- 0004(00)89115-X
    • (1995) Trends Biochem. Sci , vol.20 , pp. 495-497
    • Forsen, S.1    Linse, S.2
  • 18
    • 0034691233 scopus 로고    scopus 로고
    • Calmodulin-Peptide Interactions: Apocalmodulin Binding to the Myosin Light Chain Kinase Target-Site
    • doi: 10.1021/bi000139m
    • T.J. Hill, D. Lafitte, J.I. Wallace, H.J. Cooper, P.O. Tsvetkov and P.J. Derrick, "Calmodulin-Peptide Interactions: Apocalmodulin Binding to the Myosin Light Chain Kinase Target-Site", Biochemistry 39, 7284-7290 (2000). doi: 10.1021/bi000139m
    • (2000) Biochemistry , vol.39 , pp. 7284-7290
    • Hill, T.J.1    Lafitte, D.2    Wallace, J.I.3    Cooper, H.J.4    Tsvetkov, P.O.5    Derrick, P.J.6
  • 19
    • 33645854059 scopus 로고    scopus 로고
    • Melittin inhibits vascular smooth muscle cell proliferation through induction of apoptosis via suppression of NF-{kappa}B and Akt activation and enhancement of apoptotic protein expression
    • doi: 10.1124/jpet.105.095901
    • D.J. Son, S.J. Ha, H.S. Song, Y. Lim, Y.P. Yun, D.C. Moon, Y.H. Park, B.S. Park, M.J. Song and J.T. Hong, "Melittin inhibits vascular smooth muscle cell proliferation through induction of apoptosis via suppression of NF-{kappa}B and Akt activation and enhancement of apoptotic protein expression", J Pharmacol Exp Ther. 317, 627-634 (2006). doi: 10.1124/jpet.105.095901
    • (2006) J Pharmacol Exp Ther , vol.317 , pp. 627-634
    • Son, D.J.1    Ha, S.J.2    Song, H.S.3    Lim, Y.4    Yun, Y.P.5    Moon, D.C.6    Park, Y.H.7    Park, B.S.8    Song, M.J.9    Hong, J.T.10
  • 20
    • 0021078714 scopus 로고
    • Structural Changes in Melittin and Calmodulin upon Complex Formation and Their Modulation by Calcium
    • doi: 10.1021/bi00293a035
    • Y. Maulet and J.A. Cox, "Structural Changes in Melittin and Calmodulin upon Complex Formation and Their Modulation by Calcium", Biochemistry 22, 5680-5686 (1983). doi: 10.1021/bi00293a035
    • (1983) Biochemistry , vol.22 , pp. 5680-5686
    • Maulet, Y.1    Cox, J.A.2
  • 21
    • 36348986350 scopus 로고    scopus 로고
    • A new approach to protein structural studies using chemical cross-linking and top-down Fourier transform mass spectrometry
    • J.S. Schoeniger, G. Kruppa, P. Novak and M. Young, "A new approach to protein structural studies using chemical cross-linking and top-down Fourier transform mass spectrometry", Biophys. J. Part 2 Suppl. S 84, 356A-356A (2003).
    • (2003) Biophys. J. Part 2 Suppl. S , vol.84
    • Schoeniger, J.S.1    Kruppa, G.2    Novak, P.3    Young, M.4
  • 22
    • 0036172167 scopus 로고    scopus 로고
    • Geno3D: Automatic comparative molecular modelling of protein
    • doi: 10.1093/bioinformatics/18.1.213
    • C. Combet, M. Jambon, G. Deleage and C. Geourjon, "Geno3D: automatic comparative molecular modelling of protein", Bioinformatics 18, 213-214, (2002). doi: 10.1093/bioinformatics/18.1.213
    • (2002) Bioinformatics , vol.18 , pp. 213-214
    • Combet, C.1    Jambon, M.2    Deleage, G.3    Geourjon, C.4
  • 23
    • 36348970832 scopus 로고    scopus 로고
    • Spartan '06, Wavefunction, Inc., Irvine, CA, (USA).
    • Spartan '06, Wavefunction, Inc., Irvine, CA, (USA).
  • 25
    • 1942470540 scopus 로고    scopus 로고
    • Mapping the Topology and Determination of a Low-Resolution Three-Dimensional Structure of the Calmodulin-Melittin Complex by Chemical Cross-Linking and High-Resolution FT-ICRMS: Direct Demonstration of Multiple Binding Modes
    • doi: 10.1021/bi036149f
    • D.M. Schulz, C. Ihling, G.M Clore and A Sinz, "Mapping the Topology and Determination of a Low-Resolution Three-Dimensional Structure of the Calmodulin-Melittin Complex by Chemical Cross-Linking and High-Resolution FT-ICRMS: Direct Demonstration of Multiple Binding Modes", Biochemistry 43, 4703-4715 (2004). doi: 10.1021/bi036149f
    • (2004) Biochemistry , vol.43 , pp. 4703-4715
    • Schulz, D.M.1    Ihling, C.2    Clore, G.M.3    Sinz, A.4
  • 26
    • 0035958004 scopus 로고    scopus 로고
    • Energetics of target peptide binding by calmodulin reveals different modes of binding
    • doi: 10.1074/jbc.M010328200
    • R.D. Brokx, M.M. Lopez, H.J. Vogel and G.I. Makhatadze, "Energetics of target peptide binding by calmodulin reveals different modes of binding", J. Biol. Chem. 276, 14083-14091 (2001). doi: 10.1074/jbc.M010328200
    • (2001) J. Biol. Chem , vol.276 , pp. 14083-14091
    • Brokx, R.D.1    Lopez, M.M.2    Vogel, H.J.3    Makhatadze, G.I.4
  • 27
    • 0842286010 scopus 로고    scopus 로고
    • A top-down approach to protein structure studies using chemical cross-linking and Fourier transform mass spectrometry
    • doi: 10.1255/ejms.590
    • P. Novak, M.M. Young, J.S. Schoeniger and G.H. Kruppa, "A top-down approach to protein structure studies using chemical cross-linking and Fourier transform mass spectrometry", Eur. J. Mass Spectrom. 9, 623-631 (2003). doi: 10.1255/ejms.590
    • (2003) Eur. J. Mass Spectrom , vol.9 , pp. 623-631
    • Novak, P.1    Young, M.M.2    Schoeniger, J.S.3    Kruppa, G.H.4
  • 28
    • 33744468254 scopus 로고    scopus 로고
    • Structure and dynamics of dark-state bovine rhodopsin revealed by chemical cross-linking and high-resolution mass spectrometry
    • doi: 10.1110/ps.052040406
    • R.B. Jacobsen, K.L. Sale, M.J. Ayson, P. Novak, J. Hong, P. Lane, N.L. Wood, G.H. Kruppa, M.M. Young, and J.S. Schoeniger, "Structure and dynamics of dark-state bovine rhodopsin revealed by chemical cross-linking and high-resolution mass spectrometry", Protein Sci. 15, 1303-1317 (2006). doi: 10.1110/ps.052040406
    • (2006) Protein Sci , vol.15 , pp. 1303-1317
    • Jacobsen, R.B.1    Sale, K.L.2    Ayson, M.J.3    Novak, P.4    Hong, J.5    Lane, P.6    Wood, N.L.7    Kruppa, G.H.8    Young, M.M.9    Schoeniger, J.S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.