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Volumn 43, Issue 31, 2004, Pages 10039-10049

Structural studies on the Ca2+-binding domain of human nucleobindin (calnuc)

Author keywords

[No Author keywords available]

Indexed keywords

BIODIVERSITY; DNA; DYNAMICS; NUCLEAR MAGNETIC RESONANCE; STRUCTURAL ANALYSIS;

EID: 3543055755     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049310a     Document Type: Article
Times cited : (33)

References (60)
  • 1
  • 2
    • 0026657729 scopus 로고
    • Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure
    • Miura, K., Titani, K., Kurosawa, Y., and Kanai, Y. (1992) Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure, Biochem. Biophys. Res. Commun. 187, 375-380.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 375-380
    • Miura, K.1    Titani, K.2    Kurosawa, Y.3    Kanai, Y.4
  • 5
    • 0035909784 scopus 로고    scopus 로고
    • Gαi3 binding to calnuc on Golgi membranes in living cells monitored by fluorescence resonance energy transfer of green fluorescent protein fusion proteins
    • Weiss, T. S., Chamberlain, C. E., Takeda, T., Lin, P., Hahn, K. M., and Farquhar, M. G. (2001) Gαi3 binding to calnuc on Golgi membranes in living cells monitored by fluorescence resonance energy transfer of green fluorescent protein fusion proteins, Proc. Natl. Acad. Sci. U.S.A. 98, 14961-14966.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14961-14966
    • Weiss, T.S.1    Chamberlain, C.E.2    Takeda, T.3    Lin, P.4    Hahn, K.M.5    Farquhar, M.G.6
  • 7
    • 0036843752 scopus 로고    scopus 로고
    • 2+-binding protein, is stored and processed in the Golgi and secreted by the constitutive-like pathway in AtT20 cells
    • 2+-binding protein, is stored and processed in the Golgi and secreted by the constitutive-like pathway in AtT20 cells, Mol. Endocrinol. 16, 2462-2474.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2462-2474
    • Lavoie, C.1    Meerloo, T.2    Lin, P.3    Farquhar, M.G.4
  • 8
    • 0029130768 scopus 로고
    • Interaction of the protein nucleobindin with Gαi2, as revealed by the yeast two-hybrid system
    • Mochizuki, N., Hibi, M., Kanai, Y., and Insel, P. A. (1995) Interaction of the protein nucleobindin with Gαi2, as revealed by the yeast two-hybrid system, FEBS Lett. 373, 155-158.
    • (1995) FEBS Lett. , vol.373 , pp. 155-158
    • Mochizuki, N.1    Hibi, M.2    Kanai, Y.3    Insel, P.A.4
  • 9
    • 0028357838 scopus 로고
    • Calcium-binding activity of nucleobindin mediated by an EF hand moiety
    • Miura, K., Kurosawa, Y., and Kanai, Y. (1994) Calcium-binding activity of nucleobindin mediated by an EF hand moiety, Biochem. Biophys. Res. Commun. 199, 1388-1393.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1388-1393
    • Miura, K.1    Kurosawa, Y.2    Kanai, Y.3
  • 10
    • 0028965878 scopus 로고
    • Isolation, characterization, and primary structure of a calcium-binding 63-kDa bone protein
    • Wendel, M., Sommarin, Y., Bergman, T., and Heinegard, D. (1995) Isolation, characterization, and primary structure of a calcium-binding 63-kDa bone protein, J. Biol. Chem. 270, 6125-6133.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6125-6133
    • Wendel, M.1    Sommarin, Y.2    Bergman, T.3    Heinegard, D.4
  • 11
    • 0028903382 scopus 로고
    • Induction of autoantibodies in normal mice by injection of nucleobindin and natural occurrence of antibodies against nucleobindin in autoimmune MRL/lpr/lpr mice
    • Kanai, Y., Takeda, T., Miura, K., Amagai, M., Kanedo, T., Kubota, T., Kanai, Y., Tanuma, S.-I., and Kurosawa, Y. (1995) Induction of autoantibodies in normal mice by injection of nucleobindin and natural occurrence of antibodies against nucleobindin in autoimmune MRL/lpr/lpr mice, Immunol. Lett. 45, 35-42.
    • (1995) Immunol. Lett. , vol.45 , pp. 35-42
    • Kanai, Y.1    Takeda, T.2    Miura, K.3    Amagai, M.4    Kanedo, T.5    Kubota, T.6    Kanai, Y.7    Tanuma, S.-I.8    Kurosawa, Y.9
  • 12
    • 0029045873 scopus 로고
    • Induction and natural occurrence of serum nucleosomal DNA in autoimmune MRL/lpr/lpr mice: Its relation to apoptosis in the thymus
    • Kanai, Y., Kyuwa, S., Miura, K., and Kurosawa, Y. (1995) Induction and natural occurrence of serum nucleosomal DNA in autoimmune MRL/lpr/lpr mice: its relation to apoptosis in the thymus, Immunol. Lett. 46, 207-214.
    • (1995) Immunol. Lett. , vol.46 , pp. 207-214
    • Kanai, Y.1    Kyuwa, S.2    Miura, K.3    Kurosawa, Y.4
  • 14
    • 0034644744 scopus 로고    scopus 로고
    • The postmitotic growth suppressor necdin interacts with a calcium-binding protein (NEFA) in neuronal cytoplasm
    • Taniguchi, N., Taniura, H., Niinobe, M., Takayama, C., Tominaga-Yoshino, K., Ogura, A., and Yoshikawa, K. (2000) The postmitotic growth suppressor necdin interacts with a calcium-binding protein (NEFA) in neuronal cytoplasm, J. Biol. Chem. 275, 31674-31681.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31674-31681
    • Taniguchi, N.1    Taniura, H.2    Niinobe, M.3    Takayama, C.4    Tominaga-Yoshino, K.5    Ogura, A.6    Yoshikawa, K.7
  • 15
    • 0038636709 scopus 로고    scopus 로고
    • (Klee, E. C. a. C., Ed.), Oxford University Press, New York
    • Slupsky, C. M., and Sykes, B. D. (1999) in Calcium as a cellular regulator (Klee, E. C. a. C., Ed.) pp 73-99, Oxford University Press, New York.
    • (1999) Calcium as a Cellular Regulator , pp. 73-99
    • Slupsky, C.M.1    Sykes, B.D.2
  • 16
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax, A., and Grzesiek, S. (1993) Methodological advances in protein NMR, Acc. Chem. Res. 26, 131-138.
    • (1993) Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 17
    • 0032185144 scopus 로고    scopus 로고
    • Measurement of dipolar couplings from methylene and methyl sites in weakly oriented macromolecules and their use in structure determination
    • Ottiger, M., Delaglio, F., Marquardt, J. L., Tjandra, N., and Bax, A. (1998) Measurement of dipolar couplings from methylene and methyl sites in weakly oriented macromolecules and their use in structure determination, J. Magn. Reson. 134, 365-369.
    • (1998) J. Magn. Reson. , vol.134 , pp. 365-369
    • Ottiger, M.1    Delaglio, F.2    Marquardt, J.L.3    Tjandra, N.4    Bax, A.5
  • 18
    • 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
  • 19
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two-, three-and four dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett, D. S., Powers, R., Gronenborn, A. M., and Clore, G. M. (1991) A common sense approach to peak picking in two-, three-and four dimensional spectra using automatic computer analysis of contour diagrams, J. Magn. Reson. 95, 214-220.
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 20
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion, D., Ikura, M., Tschudin, R., and Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins, J. Magn. Reson. 85, 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 21
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible, Biochemistry 31, 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 22
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 23
    • 0001594959 scopus 로고
    • Optimized recording of heteronuclear multidimensional NMR spectra using pulse field gradients
    • Bax, A., and Pochapsky, S. S. (1992) Optimized recording of heteronuclear multidimensional NMR spectra using pulse field gradients, J. Magn. Reson. 99, 638-643.
    • (1992) J. Magn. Reson. , vol.99 , pp. 638-643
    • Bax, A.1    Pochapsky, S.S.2
  • 25
    • 0001475618 scopus 로고
    • Improved accuracy of heteronuclear transverse relaxation time measurements in macromolecules. Elimination of antiphase contributions
    • Peng, J. W., Thanabal, V., and Wagner, G. (1991) Improved accuracy of heteronuclear transverse relaxation time measurements in macromolecules. Elimination of antiphase contributions, J. Magn. Reson. 95, 421-427.
    • (1991) J. Magn. Reson. , vol.95 , pp. 421-427
    • Peng, J.W.1    Thanabal, V.2    Wagner, G.3
  • 26
    • 0027787894 scopus 로고
    • The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements
    • Grzesiek, S., and Bax, A. (1993) The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements, J. Am. Chem. Soc. 115, 12593-12594.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 29
    • 0032113480 scopus 로고    scopus 로고
    • A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
    • Clore, M. G., Gronenborn, A. M., and Bax, A. (1998) A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information, J. Magn. Reson. 133, 216-221.
    • (1998) J. Magn. Reson. , vol.133 , pp. 216-221
    • Clore, M.G.1    Gronenborn, A.M.2    Bax, A.3
  • 30
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Comilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Comilescu, G.1    Delaglio, F.2    Bax, A.3
  • 32
    • 0030856717 scopus 로고    scopus 로고
    • Calcium-induced structural transition in the regulatory domain of human cardiac troponin C
    • Spyracopoulos, L., Li, M. X., Sia, S. K., Gagne, S. M., Chandra, M., Solaro, R. J., and Sykes, B. D. (1997) Calcium-induced structural transition in the regulatory domain of human cardiac troponin C, Biochemistry 36, 12138-12146.
    • (1997) Biochemistry , vol.36 , pp. 12138-12146
    • Spyracopoulos, L.1    Li, M.X.2    Sia, S.K.3    Gagne, S.M.4    Chandra, M.5    Solaro, R.J.6    Sykes, B.D.7
  • 33
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T., and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin, Nat. Struct. Biol. 2, 758-767.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 34
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Relationship between Nuclear Magnetic Resonance Chemical Shift and Protein Secondary Structure, J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 37
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of beta-turn in proteins
    • Wilmot, C. M., and Thornton, J. M. (1988) Analysis and prediction of the different types of beta-turn in proteins, J. Mol. Biol. 203, 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 38
    • 0032708680 scopus 로고    scopus 로고
    • Diversity of conformational states and changes within the EF-hand protein superfamily
    • Yap, K. L., Ames, J. B., Swindells, M. B., and Ikura, M. (1999) Diversity of conformational states and changes within the EF-hand protein superfamily, Proteins 37, 499-507.
    • (1999) Proteins , vol.37 , pp. 499-507
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4
  • 39
    • 0028819841 scopus 로고
    • Target sequence recognition by the calmodulin superfamily: Implications from the light chain binding to the regulatory domain of scallop myosin
    • Houdusse, A., and Cohen, C. (1995) Target sequence recognition by the calmodulin superfamily: implications from the light chain binding to the regulatory domain of scallop myosin, Proc. Natl. Acad. Sci. U.S.A. 92, 10644-10647.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10644-10647
    • Houdusse, A.1    Cohen, C.2
  • 40
    • 0029149085 scopus 로고
    • Molecualr and structural basis of target recognition by calmodulin
    • Crivici, A., and Ikura, M. (1995) Molecualr and structural basis of target recognition by calmodulin, Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 41
    • 0036359353 scopus 로고    scopus 로고
    • Vector geometry mapping. A method to characterize the conformation of helix-loop-helix calcium-binding proteins
    • Yap, K. L., Ames, J. B., Swindells, M. B., and Ikura, M. (2002) Vector geometry mapping. A method to characterize the conformation of helix-loop-helix calcium-binding proteins, Methods Mol. Biol. 173, 317-324.
    • (2002) Methods Mol. Biol. , vol.173 , pp. 317-324
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4
  • 42
    • 0026596929 scopus 로고
    • 9k determined by nucleoar magnetic resonance spectroscopy
    • 9k determined by nucleoar magnetic resonance spectroscopy, Biochemistry 31, 1011-1020.
    • (1992) Biochemistry , vol.31 , pp. 1011-1020
    • Akke, M.1    Drakenberg, T.2    Chazin, W.J.3
  • 45
    • 0019074845 scopus 로고
    • Strategies for the use of lanthanide NMR shift probes in the determination of protein structure in solution. Application to the EF calcium binding site of carp parvalbumin
    • Lee, L., and Sykes, B. D. (1980) Strategies for the use of lanthanide NMR shift probes in the determination of protein structure in solution. Application to the EF calcium binding site of carp parvalbumin, Biophys. J. 32, 193-210.
    • (1980) Biophys. J. , vol.32 , pp. 193-210
    • Lee, L.1    Sykes, B.D.2
  • 46
    • 0038723707 scopus 로고    scopus 로고
    • Tuning the affinity for lanthanides of calcium binding proteins
    • Bertini, I., Gelis, I., Katsaros, N., Luchinat, C., and Provenzani, A. (2003) Tuning the affinity for lanthanides of calcium binding proteins, Biochemistry 42, 8011-8021.
    • (2003) Biochemistry , vol.42 , pp. 8011-8021
    • Bertini, I.1    Gelis, I.2    Katsaros, N.3    Luchinat, C.4    Provenzani, A.5
  • 47
    • 0033527588 scopus 로고    scopus 로고
    • Structural dynamics in the C-terminal domain of calmodulin at low calcium levels
    • Malmendal, A., Evenas, J., Forsen, S., and Akke, M. (1999) Structural dynamics in the C-terminal domain of calmodulin at low calcium levels, J. Mol. Biol. 293, 883-899.
    • (1999) J. Mol. Biol. , vol.293 , pp. 883-899
    • Malmendal, A.1    Evenas, J.2    Forsen, S.3    Akke, M.4
  • 49
    • 0034977075 scopus 로고    scopus 로고
    • 15N relaxation at four fields, reveals unique mobility characteristics of the intermotif linker
    • 15N relaxation at four fields, reveals unique mobility characteristics of the intermotif linker, Protein Sci. 10, 1393-1402.
    • (2001) Protein Sci. , vol.10 , pp. 1393-1402
    • Theret, I.1    Cox, J.A.2    Mispelter, J.3    Craescu, C.T.4
  • 51
    • 0035940465 scopus 로고    scopus 로고
    • Temperature dependence of dynamics and thermodynamics of the regulatory domain of human cardiac troponin C
    • Spyracopoulos, L., Lavigne, P., Crump, M. P., Gagne, S. M., Kay, C. M., and Sykes, B. D. (2001) Temperature dependence of dynamics and thermodynamics of the regulatory domain of human cardiac troponin C, Biochemistry 40, 12541-12551.
    • (2001) Biochemistry , vol.40 , pp. 12541-12551
    • Spyracopoulos, L.1    Lavigne, P.2    Crump, M.P.3    Gagne, S.M.4    Kay, C.M.5    Sykes, B.D.6
  • 55
    • 17344390549 scopus 로고    scopus 로고
    • Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement
    • Theret, I., Baladi, S., Cox, J. A., Sakamoto, H., and Craescu, C. T. (2000) Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement, Biochemistry 39, 7920-7926.
    • (2000) Biochemistry , vol.39 , pp. 7920-7926
    • Theret, I.1    Baladi, S.2    Cox, J.A.3    Sakamoto, H.4    Craescu, C.T.5
  • 56
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., and Lansbury, P. T. J. (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded, Biochemistry 35, 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.J.5
  • 57
    • 0033524432 scopus 로고    scopus 로고
    • Manganese stabilizing protein of photosystem II is a thermostable, natively unfolded polypetide
    • Lydakis-Simantiris, N., Hutchison, R. S., Betts, S. D., Barry, B. A., and Yocum, C. F. (1999) Manganese stabilizing protein of photosystem II is a thermostable, natively unfolded polypetide, Biochemistry 38, 404-414.
    • (1999) Biochemistry , vol.38 , pp. 404-414
    • Lydakis-Simantiris, N.1    Hutchison, R.S.2    Betts, S.D.3    Barry, B.A.4    Yocum, C.F.5
  • 58
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullman, 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    Rullman, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 59
    • 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. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 60
    • 0034257929 scopus 로고    scopus 로고
    • 2+-bound calmodulin: An analysis of disorder and implications for functionally relevant plasticity
    • 2+-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity, J. Mol. Biol. 301, 1237-1256.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1237-1256
    • Wilson, M.A.1    Brunger, A.T.2


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