메뉴 건너뛰기




Volumn 328, Issue 2, 2003, Pages 365-383

Structural features of human initiation factor 4E, studied by X-ray crystal analyses and molecular dynamics simulations

Author keywords

Initiation factor 4E; m7GpppA; m7GTP; Molecular dynamics simulation; X ray crystal structure

Indexed keywords

ADENOSINE; INITIATION FACTOR 4E; MESSENGER RNA; NUCLEOTIDE; PHOSPHATE; TRIPHOSPHATE; UNCLASSIFIED DRUG; WATER;

EID: 0037466314     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00314-0     Document Type: Article
Times cited : (87)

References (44)
  • 1
    • 0019437882 scopus 로고
    • The cap structure in eukaryotic messenger RNA as a mark of a strand carrying protein information
    • Miura K. The cap structure in eukaryotic messenger RNA as a mark of a strand carrying protein information. Advan. Biophys. 14:1981;205-238.
    • (1981) Advan. Biophys. , vol.14 , pp. 205-238
    • Miura, K.1
  • 2
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain V.M. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236:1996;747-771.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 3
    • 0000831271 scopus 로고    scopus 로고
    • MRNA 5′cap-binding protein eIF4E and control of cell growth
    • N. Sonenberg. New York: Cold Spring Harbor Laboratory Press
    • Sonenberg N. mRNA 5′cap-binding protein eIF4E and control of cell growth. Sonenberg N. Transcriptional Control. 1996;245-269 Cold Spring Harbor Laboratory Press, New York.
    • (1996) Transcriptional Control , pp. 245-269
    • Sonenberg, N.1
  • 4
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano J., Gingras A.C., Sonenberg N., Burley S.K. Cocrystal structure of the messenger RNA 5′cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell. 89:1997;951-961.
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 6
    • 0034760120 scopus 로고    scopus 로고
    • Structural and thermodynamic behavior of eukaryotic initiation factor 4E in supramolecular formation with 4E-binding protein 1 and mRNA cap analogue, studied by spectroscopic methods
    • Shen X., Tomoo K., Uchiyama S., Kobayashi Y., Ishida T. Structural and thermodynamic behavior of eukaryotic initiation factor 4E in supramolecular formation with 4E-binding protein 1 and mRNA cap analogue, studied by spectroscopic methods. Chem. Pharm. Bull. 49:2001;1299-1303.
    • (2001) Chem. Pharm. Bull. , vol.49 , pp. 1299-1303
    • Shen, X.1    Tomoo, K.2    Uchiyama, S.3    Kobayashi, Y.4    Ishida, T.5
  • 7
    • 0037086471 scopus 로고    scopus 로고
    • 7GpppA)-bound human full-length eukaryotic initation factor 4E: Biological importance of the C-terminal flexible region
    • 7GpppA)-bound human full-length eukaryotic initation factor 4E: biological importance of the C-terminal flexible region. Biochem. J. 362:2002;539-544.
    • (2002) Biochem. J. , vol.362 , pp. 539-544
    • Tomoo, K.1    Shen, X.2    Okabe, K.3    Nozoe, Y.4    Fukuhara, S.5    Morino, S.6
  • 10
    • 0023929705 scopus 로고
    • Specific ring stacking interaction on the tryptophan-7-methylguanine system: Comparative crystallographic studies of indole derivatives-7-methylguanine base, nucleoside, and nucleotide complexes
    • Ishida T., Doi M., Ueda H., Inoue M., Scheldrick G.M. Specific ring stacking interaction on the tryptophan-7-methylguanine system: comparative crystallographic studies of indole derivatives-7-methylguanine base, nucleoside, and nucleotide complexes. J. Am. Chem. Soc. 110:1988;2286-2294.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 2286-2294
    • Ishida, T.1    Doi, M.2    Ueda, H.3    Inoue, M.4    Scheldrick, G.M.5
  • 11
    • 37049079318 scopus 로고
    • Importance of simultaneous co-operation of hydrogen bond pairing and stacking interactions for recognition of guanine base by a peptide: X-ray crystal analysis of 7-methylguanosine-5′-phosphate-tryptophanylglutamic acid complex
    • Ishida T., Iyo H., Ueda H., Doi M., Inoue M., Nishimura S., Kitamura K. Importance of simultaneous co-operation of hydrogen bond pairing and stacking interactions for recognition of guanine base by a peptide: X-ray crystal analysis of 7-methylguanosine-5′-phosphate-tryptophanylglutamic acid complex. J. Chem. Soc. Perkin Trans. 1. 1991;1847-1853.
    • (1991) J. Chem. Soc. Perkin Trans. 1 , pp. 1847-1853
    • Ishida, T.1    Iyo, H.2    Ueda, H.3    Doi, M.4    Inoue, M.5    Nishimura, S.6    Kitamura, K.7
  • 12
    • 0036307897 scopus 로고    scopus 로고
    • Biophysical studies of eIF4E cap-binding protein: Recognition of mRNA 5′ cap structure and synthetic fragments of eIF4G and 4E-BP1 proteins
    • Niedzwiecka A., Marcotrigiano J., Stepinski J., Jankowska-Anyszka M., Wyslouch-Cieszynska A., Dadlez M., et al. Biophysical studies of eIF4E cap-binding protein: recognition of mRNA 5′ cap structure and synthetic fragments of eIF4G and 4E-BP1 proteins. J. Mol. Biol. 319:2002;615-635.
    • (2002) J. Mol. Biol. , vol.319 , pp. 615-635
    • Niedzwiecka, A.1    Marcotrigiano, J.2    Stepinski, J.3    Jankowska-Anyszka, M.4    Wyslouch-Cieszynska, A.5    Dadlez, M.6
  • 14
    • 0029949032 scopus 로고    scopus 로고
    • Analysis of the mRNA cap-binding ability of human eukaryotic initiation factor-4E by use of recombinant wild-type and mutant forms
    • Morino S., Hazama H., Ozaki M., Teraoka Y., Shibata S., Doi M., et al. Analysis of the mRNA cap-binding ability of human eukaryotic initiation factor-4E by use of recombinant wild-type and mutant forms. Eur. J. Biochem. 239:1996;597-601.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 597-601
    • Morino, S.1    Hazama, H.2    Ozaki, M.3    Teraoka, Y.4    Shibata, S.5    Doi, M.6
  • 15
    • 0024297272 scopus 로고
    • Site-directed mutagenesis of the tryptophan residues in yeast eukaryotic initiation factor 4E
    • Altmann A., Edery I., Trachsel H., Sonenberg N. Site-directed mutagenesis of the tryptophan residues in yeast eukaryotic initiation factor 4E. J. Biol. Chem. 263:1988;17229-17232.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17229-17232
    • Altmann, A.1    Edery, I.2    Trachsel, H.3    Sonenberg, N.4
  • 17
    • 0032079873 scopus 로고    scopus 로고
    • Regulation of translation initiation factors by signal transduction
    • Kleijn M., Scheper G.C., Voorma H.O., Thomas A.A.M. Regulation of translation initiation factors by signal transduction. Eur. J. Biochem. 253:1998;531-544.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 531-544
    • Kleijn, M.1    Scheper, G.C.2    Voorma, H.O.3    Thomas, A.A.M.4
  • 18
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • Minich W.B., Balasta M.L., Goss D.J., Rhoads R.E. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc. Natl Acad. Sci. USA. 91:1994;7668-7672.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 19
    • 0036479313 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initation factor 4E markedly reduces its affinity for capped mRNA
    • Scheper G.C., van Kollenburg B., Hu J., Luo Y., Goss D.J., Proud C.G. Phosphorylation of eukaryotic initation factor 4E markedly reduces its affinity for capped mRNA. J. Biol. Chem. 277:2002;3303-3309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3303-3309
    • Scheper, G.C.1    Van Kollenburg, B.2    Hu, J.3    Luo, Y.4    Goss, D.J.5    Proud, C.G.6
  • 20
    • 0032543347 scopus 로고    scopus 로고
    • Effect of mRNA cap structure on eIF-4E phosphorylation and cap binding analyses using Ser209-mutated eIF-4Es
    • Shibata S., Morino S., Tomoo K., In Y., Ishida T. Effect of mRNA cap structure on eIF-4E phosphorylation and cap binding analyses using Ser209-mutated eIF-4Es. Biochem. Biophys. Res. Commun. 247:1998;213-216.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 213-216
    • Shibata, S.1    Morino, S.2    Tomoo, K.3    In, Y.4    Ishida, T.5
  • 21
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause A., Belsham G.J., Gingras A.C., Donze O., Lin T.A., Lawrence J. Jr, Sonenberg N. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature. 371:1994;762-767.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence J., Jr.6    Sonenberg, N.7
  • 22
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano J., Gingras A.C., Sonenberg N., Burley S.K. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell. 3:1999;707-716.
    • (1999) Mol. Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 25
    • 0028048713 scopus 로고
    • Direct expression of a synthetic gene in Escherichia coli: Purification and physicochemical properties of human initiation factor 4E
    • Morino S., Yasui M., Doi M., Inoue M., Ishida T., Ueda H., Uesugi S. Direct expression of a synthetic gene in Escherichia coli: purification and physicochemical properties of human initiation factor 4E. J. Biochem. 116:1994;687-693.
    • (1994) J. Biochem. , vol.116 , pp. 687-693
    • Morino, S.1    Yasui, M.2    Doi, M.3    Inoue, M.4    Ishida, T.5    Ueda, H.6    Uesugi, S.7
  • 26
    • 0002193613 scopus 로고
    • The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography
    • Higashi T. The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography. J. Appl. Crystallog. 22:1989;9-18.
    • (1989) J. Appl. Crystallog. , vol.22 , pp. 9-18
    • Higashi, T.1
  • 27
    • 0030041898 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction study of recombinant human eukaryotic initiation factor-4E
    • Morino S., Tomoo K., Nishi N., Okabe K., Doi M., Ishida T., Mitamura K. Crystallization and preliminary X-ray diffraction study of recombinant human eukaryotic initiation factor-4E. J. Biochem. 119:1996;224-225.
    • (1996) J. Biochem. , vol.119 , pp. 224-225
    • Morino, S.1    Tomoo, K.2    Nishi, N.3    Okabe, K.4    Doi, M.5    Ishida, T.6    Mitamura, K.7
  • 29
    • 0000356658 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones T.A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 15:1978;23-31.
    • (1978) J. Appl. Crystallog. , vol.15 , pp. 23-31
    • Jones, T.A.1
  • 31
    • 0029011701 scopus 로고
    • A second generations force field for the simulations of proteins, nucleic acids, and organic molecules
    • Cornell W.D., Cieplak P., Bayly C.I., Gould I.R., Merz K.M. Jr, Ferguson D.M., et al. A second generations force field for the simulations of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117:1995;5179-5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3    Gould, I.R.4    Merz K.M., Jr.5    Ferguson, D.M.6
  • 32
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - A rapid access to atomic charges
    • Gasteiger J., Marsili M. Iterative partial equalization of orbital electronegativity - a rapid access to atomic charges. Tetrahedron. 36:1980;3219-3288.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3288
    • Gasteiger, J.1    Marsili, M.2
  • 33
    • 17144471008 scopus 로고    scopus 로고
    • Comparison of different schemes to treat long-range electrostatic interactions in molecular dynamics simulations of a protein crystal
    • Walser R., Hunenberger P.H., van Gunsteren W.F. Comparison of different schemes to treat long-range electrostatic interactions in molecular dynamics simulations of a protein crystal. Proteins: Struct. Funct. Genet. 43:2001;509-519.
    • (2001) Proteins: Struct. Funct. Genet. , vol.43 , pp. 509-519
    • Walser, R.1    Hunenberger, P.H.2    Van Gunsteren, W.F.3
  • 34
    • 0036681338 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a double unit cell in a protein crystal: Volume relaxation at constant pressure and correlation of motions between the two unit cells
    • Walser R., Hunenberger P.H., van Gunsteren W.F. Molecular dynamics simulations of a double unit cell in a protein crystal: volume relaxation at constant pressure and correlation of motions between the two unit cells. Proteins: Struct. Funct. Genet. 48:2002;327-340.
    • (2002) Proteins: Struct. Funct. Genet. , vol.48 , pp. 327-340
    • Walser, R.1    Hunenberger, P.H.2    Van Gunsteren, W.F.3
  • 35
    • 14244271476 scopus 로고    scopus 로고
    • Molecular dynamics simulation of nucleic acids: Successes, limitations, and promise
    • Cheatham T.E. III, Young M.A. Molecular dynamics simulation of nucleic acids: successes, limitations, and promise. Biopolymers. 56:2001;232-256.
    • (2001) Biopolymers , vol.56 , pp. 232-256
    • Cheatham T.E. III1    Young, M.A.2
  • 37
    • 0001700958 scopus 로고    scopus 로고
    • Development of MD engine: High-speed accelerator with parallel processor design for molecular dynamics simulations
    • Toyoda S., Miyagawa H., Kitamura K., Amisaki T., Hashimoto E., Ikeda H., et al. Development of MD engine: high-speed accelerator with parallel processor design for molecular dynamics simulations. J. Comput. Chem. 20:1999;185-199.
    • (1999) J. Comput. Chem. , vol.20 , pp. 185-199
    • Toyoda, S.1    Miyagawa, H.2    Kitamura, K.3    Amisaki, T.4    Hashimoto, E.5    Ikeda, H.6
  • 40
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert J.P., Ciccotti G., Berendsen H.J.C. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23:1977;327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 41
    • 0028143603 scopus 로고
    • Characterization of the transition state of protein unfolding by use of molecular dynamics: Chymotrypsin inhibitor 2
    • Li A., Daggett V. Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2. Proc. Natl Acad. Sci. 91:1994;10430-10434.
    • (1994) Proc. Natl Acad. Sci. , vol.91 , pp. 10430-10434
    • Li, A.1    Daggett, V.2
  • 42
    • 0036784640 scopus 로고    scopus 로고
    • Conformational transition states of a beta-hairpin peptide between the ordered and disordered conformations in explicit water
    • Kamiya N., Higo J., Nakamura H. Conformational transition states of a beta-hairpin peptide between the ordered and disordered conformations in explicit water. Protein Sci. 11:2002;2297-2307.
    • (2002) Protein Sci. , vol.11 , pp. 2297-2307
    • Kamiya, N.1    Higo, J.2    Nakamura, H.3
  • 43
    • 0000243829 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallog. 26:1991;282-291.
    • (1991) J. Appl. Crystallog. , vol.26 , pp. 282-291
    • Kraulis, P.1
  • 44
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Meritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Meritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.