메뉴 건너뛰기




Volumn 274, Issue 4, 1997, Pages 661-675

The three-dimensional high resolution structure of human interferon α-2a determined by heteronuclear NMR spectroscopy in solution

Author keywords

Cytokine; Four helix bundle; Interferon ; NMR spectroscopy; Protein structure

Indexed keywords

ALPHA2A INTERFERON; ALPHA2B INTERFERON; BETA INTERFERON; CYTOKINE; DISULFIDE; METHYL GROUP; NITROGEN 15; RECOMBINANT ALPHA2A INTERFERON;

EID: 0031566032     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1396     Document Type: Article
Times cited : (158)

References (62)
  • 4
    • 0001677570 scopus 로고
    • Isotope-filtered 2D HOHAHA spectroscopy of a peptide-protein complex using heteronuclear Hartmann-Hahn dephasing
    • Bax A., Grzesiek D., Gronenborn A. M., Clore G. M. Isotope-filtered 2D HOHAHA spectroscopy of a peptide-protein complex using heteronuclear Hartmann-Hahn dephasing. J. Magn. Reson. ser. A. 106:1994a;269-273.
    • (1994) J. Magn. Reson. Ser. A , vol.106 , pp. 269-273
    • Bax, A.1    Grzesiek, D.2    Gronenborn, A.M.3    Clore, G.M.4
  • 7
    • 0026525987 scopus 로고
    • Interferons-expanding therapeutic roles
    • Borden E. C. Interferons-expanding therapeutic roles. N. Engl. J. Med. 326:1992;1491-1493.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1491-1493
    • Borden, E.C.1
  • 11
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos A. M., Ultsch M., Kossiakoff A. A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 255:1992;306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 12
    • 0019800792 scopus 로고
    • Antiproliferative and antiviral activities of human leukocyte interferons
    • Evinger M., Rubinstein M., Pestka S. Antiproliferative and antiviral activities of human leukocyte interferons. Arch. Biochim. Biophys. 210:1981;319-329.
    • (1981) Arch. Biochim. Biophys. , vol.210 , pp. 319-329
    • Evinger, M.1    Rubinstein, M.2    Pestka, S.3
  • 13
    • 0026908951 scopus 로고
    • Definition of receptor binding domains in interferon-α
    • Fish E. N. Definition of receptor binding domains in interferon-α J. Interferon Res. 12:1992;257-266.
    • (1992) J. Interferon Res. , vol.12 , pp. 257-266
    • Fish, E.N.1
  • 14
    • 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., Clore G. M. A common sense approach to peak picking in two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95:1991;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
  • 15
    • 0001505364 scopus 로고
    • Superimposing several sets of atomic coordinates
    • Gerber P. R., Müller K. Superimposing several sets of atomic coordinates. Acta Crystallog. sect. A. 43:1987;426-428.
    • (1987) Acta Crystallog. Sect. A , vol.43 , pp. 426-428
    • Gerber, P.R.1    Müller, K.2
  • 16
    • 0029315603 scopus 로고
    • MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry
    • Gerber P. R., Müller K. MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry. J. Comput Aided Mol. Des. 9:1995;251-268.
    • (1995) J. Comput Aided Mol. Des. , vol.9 , pp. 251-268
    • Gerber, P.R.1    Müller, K.2
  • 17
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • Grzesiek S., Bax A. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96:1992a;432-440.
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 18
    • 44049109615 scopus 로고
    • An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins
    • Grzesiek S., Bax A. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J. Magn. Reson. 99:1992b;201-207.
    • (1992) J. Magn. Reson. , vol.99 , pp. 201-207
    • Grzesiek, S.1    Bax, A.2
  • 19
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek S., Bax A. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114:1992c;6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 26
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA, and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert P., Braun W., Wüthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA, and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217:1991;517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 27
    • 0030238916 scopus 로고    scopus 로고
    • Determination of the solution structure of the SH3 domain of human p56 Lck tyrosine kinase
    • Hiroaki H., Klaus W., Senn H. Determination of the solution structure of the SH3 domain of human p56 Lck tyrosine kinase. J. Biomol. NMR. 8:1996;105-122.
    • (1996) J. Biomol. NMR , vol.8 , pp. 105-122
    • Hiroaki, H.1    Klaus, W.2    Senn, H.3
  • 28
    • 0022854257 scopus 로고
    • Large-scale recovery of interferon α-2a synthesized in bacteria
    • Hochuli E. Large-scale recovery of interferon α-2a synthesized in bacteria. Chimia. 40:1986;408-412.
    • (1986) Chimia , vol.40 , pp. 408-412
    • Hochuli, E.1
  • 31
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander. Ch. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander., Ch.2
  • 32
    • 0024988099 scopus 로고
    • Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1β in solution
    • Kay L. E., Clore G. M., Bax A., Gronenborn A. M. Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1β in solution. Science. 249:1990;411-414.
    • (1990) Science , vol.249 , pp. 411-414
    • Kay, L.E.1    Clore, G.M.2    Bax, A.3    Gronenborn, A.M.4
  • 33
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R. A., Moss D. S., Thornton J. M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231:1993;1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 34
    • 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., Thornton J. M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;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
  • 36
    • 0027227660 scopus 로고
    • Structural, functional and evolutionary implications of the three-dimensional crystal structure of murine interferon-β
    • Mitsui Y., Senda T., Shimazu T., Matsuda S., Utsumi J. Structural, functional and evolutionary implications of the three-dimensional crystal structure of murine interferon-β Pharmac. Ther. 58:1993;93-132.
    • (1993) Pharmac. Ther. , vol.58 , pp. 93-132
    • Mitsui, Y.1    Senda, T.2    Shimazu, T.3    Matsuda, S.4    Utsumi, J.5
  • 37
    • 0028915369 scopus 로고
    • Four-helix bundle growth factors and their receptors: Protein-protein interactions
    • Mott H. R., Campbell I. D. Four-helix bundle growth factors and their receptors: protein-protein interactions. Curr. Opin. Struct. Biol. 5:1995;114-121.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 114-121
    • Mott, H.R.1    Campbell, I.D.2
  • 40
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities
    • Nilges M. Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities. J. Mol. Biol. 245:1995;645-660.
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-660
    • Nilges, M.1
  • 41
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • Nilges M., Clore G. M., Gronenborn A. M. Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Letters. 239:1988;129-136.
    • (1988) FEBS Letters , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 42
    • 0028299340 scopus 로고
    • The human interferon α/β receptor: Characterization and molecular cloning
    • Novick D., Cohen B., Rubinstein M. The human interferon α/β receptor: characterization and molecular cloning. Cell. 77:1994;391-400.
    • (1994) Cell , vol.77 , pp. 391-400
    • Novick, D.1    Cohen, B.2    Rubinstein, M.3
  • 44
    • 0024722728 scopus 로고
    • Topological distribution of four-α-helix bundles
    • Presnell S. R., Cohen F. E. Topological distribution of four-α-helix bundles. Proc. Natl Acad. Sci. USA. 86:1989;6592-6596.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6592-6596
    • Presnell, S.R.1    Cohen, F.E.2
  • 47
    • 0026739463 scopus 로고
    • The interferon system
    • Seng G. C., Lengyel P. The interferon system. J. Biol. Chem. 267:1992;5017-5020.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5017-5020
    • Seng, G.C.1    Lengyel, P.2
  • 49
    • 0028791828 scopus 로고
    • Refined crystal structure of recombinant murine interferon-β at 2.15 Å resolution
    • Senda T., Saitoh S., Mitsui Y. Refined crystal structure of recombinant murine interferon-β at 2.15 Å resolution. J. Mol. Biol. 253:1995;187-207.
    • (1995) J. Mol. Biol. , vol.253 , pp. 187-207
    • Senda, T.1    Saitoh, S.2    Mitsui, Y.3
  • 50
    • 0027165368 scopus 로고
    • The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet gpIIb-IIIa receptor
    • Senn H., Klaus W. The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet gpIIb-IIIa receptor. J. Mol. Biol. 232:1993;907-925.
    • (1993) J. Mol. Biol. , vol.232 , pp. 907-925
    • Senn, H.1    Klaus, W.2
  • 52
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J. D., Higgins D. G., Gibson T. J. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 53
    • 0025015138 scopus 로고
    • Genetic transfer of a functional human interferon α receptor into mouse cells: Cloning and expression of its cDNA
    • Uzé G., Lutfalla G., Gresser I. Genetic transfer of a functional human interferon α receptor into mouse cells: cloning and expression of its cDNA. Cell. 60:1990;225-234.
    • (1990) Cell , vol.60 , pp. 225-234
    • Uzé, G.1    Lutfalla, G.2    Gresser, I.3
  • 59
    • 0028152571 scopus 로고
    • 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotopic labeling
    • Vuister G. W., Kim S.-J., Wu C., Bax A. 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotopic labeling. J. Am. Chem. Soc. 116:1994;9206-9210.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9206-9210
    • Vuister, G.W.1    Kim, S.-J.2    Wu, C.3    Bax, A.4
  • 60
    • 0027105153 scopus 로고
    • Structure-function study of the region encompassing residues 26-40 of human interferon-α4: Identification of residues important for antiviral and antiproliferative activities
    • Waine G. J., Tymms M. J., Brandt E. R., Cheetham B. F., Linnane A. W. Structure-function study of the region encompassing residues 26-40 of human interferon-α4: identification of residues important for antiviral and antiproliferative activities. J. Interferon Res. 12:1992;43-48.
    • (1992) J. Interferon Res. , vol.12 , pp. 43-48
    • Waine, G.J.1    Tymms, M.J.2    Brandt, E.R.3    Cheetham, B.F.4    Linnane, A.W.5
  • 62
    • 0028260226 scopus 로고
    • Structural and functional basis for hormone binding and receptor oligomerization
    • Wells J. A. Structural and functional basis for hormone binding and receptor oligomerization. Curr. Opin. Cell. Biol. 6:1994;163-173.
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 163-173
    • Wells, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.