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Volumn 13, Issue 3, 2004, Pages 727-734

The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila

Author keywords

Dimerization; Domain swapping; Dynein light chain; PH induced dissociation; Protein structure

Indexed keywords

DIMER; DYNEIN ADENOSINE TRIPHOSPHATASE; MONOMER;

EID: 1342331844     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03462204     Document Type: Article
Times cited : (34)

References (37)
  • 1
    • 0035859852 scopus 로고    scopus 로고
    • NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor
    • Barbar, E., Hare, M., Makokha, M., Barany, G., and Woodward, C. 2001a. NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor. Biochemistry 40: 9734-9742.
    • (2001) Biochemistry , vol.40 , pp. 9734-9742
    • Barbar, E.1    Hare, M.2    Makokha, M.3    Barany, G.4    Woodward, C.5
  • 2
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar, E., Kleinman, B., Imhoff, D., Li, M., Hays, T., and Hare, M. 2001b. Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry 40: 1596-1605.
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.5    Hare, M.6
  • 3
    • 0028674451 scopus 로고
    • Multidimensional heteronuclear nuclear magnetic resonance of proteins
    • (eds. T.L. James and N.J. Oppenheimer), Academic Press, San Diego, CA
    • Clore, G.M. and Gronenborn, A.M. 1994. Multidimensional heteronuclear nuclear magnetic resonance of proteins. In Nuclear magnetic resonance, Part C. (eds. T.L. James and N.J. Oppenheimer), pp. 349-363. Academic Press, San Diego, CA.
    • (1994) Nuclear Magnetic Resonance, Part C , pp. 349-363
    • Clore, G.M.1    Gronenborn, A.M.2
  • 4
    • 0030613781 scopus 로고    scopus 로고
    • IκBα physically interacts with a cytoskeleton-associated protein through its signal response domain
    • Crepieux, P., Kwon, H., Leclerc, N., Spencer, W., Richard, S., Lin, R.T., and Hiscott, J. 1997. IκBα physically interacts with a cytoskeleton-associated protein through its signal response domain. Mol. Cell. Biol. 17: 7375-7385.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7375-7385
    • Crepieux, P.1    Kwon, H.2    Leclerc, N.3    Spencer, W.4    Richard, S.5    Lin, R.T.6    Hiscott, J.7
  • 5
    • 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
  • 7
    • 0035830488 scopus 로고    scopus 로고
    • Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain
    • Fan, J.S., Zhang, Q., Tochio, H., Li, M., and Zhang, M.J. 2001. Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain. J. Mol. Biol. 306: 97-108.
    • (2001) J. Mol. Biol. , vol.306 , pp. 97-108
    • Fan, J.S.1    Zhang, Q.2    Tochio, H.3    Li, M.4    Zhang, M.J.5
  • 8
    • 0035965135 scopus 로고    scopus 로고
    • Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle α-tropomyosin in an engineered chimeric protein
    • Greenfield, N.J., Huang, Y.J., Palm, T., Swapna, G.V.T., Monleon, D., Montelione, G.T., and Hitchcock-DeGregori, S.E. 2001. Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle α-tropomyosin in an engineered chimeric protein. J. Mol. Biol. 312: 833-847.
    • (2001) J. Mol. Biol. , vol.312 , pp. 833-847
    • Greenfield, N.J.1    Huang, Y.J.2    Palm, T.3    Swapna, G.V.T.4    Monleon, D.5    Montelione, G.T.6    Hitchcock-DeGregori, S.E.7
  • 9
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31-Kda protein
    • Grzesiek, S., and Bax, A. 1992. Improved 3D triple-resonance NMR techniques applied to a 31-Kda protein. J. Magn. Reson. 96: 432-440.
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 10
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization
    • Grzesiek, S., Anglister, J., and Bax, A. 1993. Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization. J. Magn. Reson. B 101: 114-119.
    • (1993) J. Magn. Reson. B , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 11
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., Mumenthaler, C., and Wuthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 12
    • 0037459257 scopus 로고    scopus 로고
    • Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli
    • Huang, Y.P.J., Swapna, G.V.T., Rajan, P.K., Ke, H.P., Xia, B., Shukla, K., Inouye, M., and Montelione, G.T. 2003. Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli. J. Mol. Biol. 327: 521-536.
    • (2003) J. Mol. Biol. , vol.327 , pp. 521-536
    • Huang, Y.P.J.1    Swapna, G.V.T.2    Rajan, P.K.3    Ke, H.P.4    Xia, B.5    Shukla, K.6    Inouye, M.7    Montelione, G.T.8
  • 13
    • 0033775766 scopus 로고    scopus 로고
    • Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
    • Jacob, Y., Badrane, H., Ceccaldi, P.E., and Tordo, N. 2000. Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. J. Virol. 74: 10217-10222.
    • (2000) J. Virol. , vol.74 , pp. 10217-10222
    • Jacob, Y.1    Badrane, H.2    Ceccaldi, P.E.3    Tordo, N.4
  • 14
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey, S.R. and Snyder, S.H. 1996. PIN: An associated protein inhibitor of neuronal nitric oxide synthase. Science 274: 774-777.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 15
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones, S. and Thornton, J.M. 1995. Protein-protein interactions: A review of protein dimer structures. Prog. Biophys. Mol. Biol. 63: 31-65.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 17
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 18
    • 0028545648 scopus 로고
    • Measurement of H-N-H-α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • Kuboniwa, H., Grzesiek, S., Delaglio, F., and Bax, A. 1994. Measurement of H-N-H-α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4: 871-878.
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 19
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Kaptein, R., and Thornton, J.M. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8: 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 20
    • 0032190305 scopus 로고    scopus 로고
    • Analytical shape computation of macromolecules. I: Molecular area and volume through α shape
    • Liang, J., Edelsbrunner, H., Fu, P., Sudhakar, P.V., and Subramaniam, S. 1998. Analytical shape computation of macromolecules, I: Molecular area and volume through α shape. Proteins 33: 1-17.
    • (1998) Proteins , vol.33 , pp. 1-17
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.V.4    Subramaniam, S.5
  • 22
    • 0037006969 scopus 로고    scopus 로고
    • Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74
    • Makokha, M., Hare, M., Li, M., Hays, T., and Barbar, E. 2002. Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74. Biochemistry 41: 4302-4311.
    • (2002) Biochemistry , vol.41 , pp. 4302-4311
    • Makokha, M.1    Hare, M.2    Li, M.3    Hays, T.4    Barbar, E.5
  • 23
    • 1442306656 scopus 로고    scopus 로고
    • Assignment validation software suite for the evaluation and presentation of protein resonance assignment data
    • in press
    • Moseley, H.N.B., Sahota, G., and Montelione, G.T. 2003. Assignment validation software suite for the evaluation and presentation of protein resonance assignment data. J. Biomol. NMR (in press).
    • (2003) J. Biomol. NMR
    • Moseley, H.N.B.1    Sahota, G.2    Montelione, G.T.3
  • 24
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D.R. and Kay, L.E. 1994. Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. B 103: 203-216.
    • (1994) J. Magn. Reson. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 25
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt, S., Valtschanoff, J., Allison, D.W., Sala, C., Kim, E., Craig, A.M., Weinberg, R.J., and Sheng, M. 2000. Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. J. Neurosci. 20: 4524-4534.
    • (2000) J. Neurosci. , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Craig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 26
    • 1342299402 scopus 로고    scopus 로고
    • Interactions of LC8 with N-terminal segments of the intermediate chain of cytoplasmic dynein
    • Nyarko, A., Hare, M., Makokha, M., and Barbar, E. 2003. Interactions of LC8 with N-terminal segments of the intermediate chain of cytoplasmic dynein. Sci. World J. 3: 647-654.
    • (2003) Sci. World J. , vol.3 , pp. 647-654
    • Nyarko, A.1    Hare, M.2    Makokha, M.3    Barbar, E.4
  • 28
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath, H., Huang, D.C.S., O'Reilly, L.A., King, S.M., and Strasser, A. 1999. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell 3: 287-296.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.S.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 29
    • 0033776043 scopus 로고    scopus 로고
    • Interaction of the rabies virus P protein with the LC8 dynein light chain
    • Raux, H., Flamand, A., and Blondel, D. 2000. Interaction of the rabies virus P protein with the LC8 dynein light chain. J. Virol. 74: 10212-10216.
    • (2000) J. Virol. , vol.74 , pp. 10212-10216
    • Raux, H.1    Flamand, A.2    Blondel, D.3
  • 30
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson, J.S. and Richardson, D.C. 2002. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. 99: 2754-2759.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 31
    • 0032533611 scopus 로고    scopus 로고
    • Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition
    • Rodriguez-Crespo, I., Straub, W., Gavilanes, F., and de Montellano, P.R.O. 1998. Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition. Arch. Biochem. Biophys. 359: 297-304.
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 297-304
    • Rodriguez-Crespo, I.1    Straub, W.2    Gavilanes, F.3    De Montellano, P.R.O.4
  • 32
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M.P., Bennett, M.J., and Eisenberg, D. 1997. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly. Adv. Protein Chem. 50: 61-122.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 33
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer, F., Bohmann, K., and Nusslein-Volhard, C. 2000. The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes. Nat. Cell Biol. 2: 185-190.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 34
    • 0031791314 scopus 로고    scopus 로고
    • Solution structure of a protein inhibitor of neuronal nitric oxide synthase
    • Tochio, H., Ohki, S., Zhang, Q., Li, M., and Zhang, M.J. 1998. Solution structure of a protein inhibitor of neuronal nitric oxide synthase. Nat. Struct. Biol. 5: 965-969.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 965-969
    • Tochio, H.1    Ohki, S.2    Zhang, Q.3    Li, M.4    Zhang, M.J.5
  • 35
    • 0142039800 scopus 로고    scopus 로고
    • Structure of the monomeric 8-kd dynein light chain and mechanism of the domain swapped dimer assembly
    • Wang, W., Lo, K.W.-H., Kan, H., Fan, J., and Zhang, M. 2003. Structure of the monomeric 8-kd dynein light chain and mechanism of the domain swapped dimer assembly. J. Biol. Chem. 278: 41491-41499.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41491-41499
    • Wang, W.1    Lo, K.W.-H.2    Kan, H.3    Fan, J.4    Zhang, M.5
  • 36
    • 0031913197 scopus 로고    scopus 로고
    • Mechanism and evolution of protein dimerization
    • Xu, D., Tsai, C.J., and Nussinov, R. 1998. Mechanism and evolution of protein dimerization. Protein Sci. 7: 533-544.
    • (1998) Protein Sci. , vol.7 , pp. 533-544
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3


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