메뉴 건너뛰기




Volumn 271, Issue 2, 1997, Pages 266-277

NMR structural studies of human cystatin C dimers and monomers

Author keywords

Amyloidosis; Cystatin C; NMR spectroscopy; Protein folding; Protein self association

Indexed keywords

AMINO ACID; AMYLOID; CYSTATIN C; CYSTEINE PROTEINASE INHIBITOR; DIMER; MONOMER;

EID: 0031571596     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1150     Document Type: Article
Times cited : (101)

References (46)
  • 1
    • 0024227598 scopus 로고
    • Human cysteine proteinase inhibitors: Isolation, physiological importance, inhibitory mechanism, gene structure and relation to hereditary cerebral hemorrhage
    • Abrahamson M. Human cysteine proteinase inhibitors: isolation, physiological importance, inhibitory mechanism, gene structure and relation to hereditary cerebral hemorrhage. Scand. J. Clin. Lab. Invest. 48 (Suppl. 191):1988;21-31.
    • (1988) Scand. J. Clin. Lab. Invest. , vol.48 , Issue.SUPPL. 191 , pp. 21-31
    • Abrahamson, M.1
  • 2
    • 0027976996 scopus 로고
    • Increased body temperature accelerates aggregation of the Leu-68 → Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy
    • Abrahamson M., Grubb A. Increased body temperature accelerates aggregation of the Leu-68 → Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy. Proc. Natl Acad. Sci. USA. 91:1994;1416-1420.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1416-1420
    • Abrahamson, M.1    Grubb, A.2
  • 3
    • 0023684074 scopus 로고
    • Efficient production of native, biologically active human cystatin C byEscherichia coli
    • Abrahamson M., Dalbøge H., Olafsson I., Carlsen S., Grubb A. Efficient production of native, biologically active human cystatin C byEscherichia coli. FEBS Letters. 236:1988;14-18.
    • (1988) FEBS Letters , vol.236 , pp. 14-18
    • Abrahamson, M.1    Dalbøge, H.2    Olafsson, I.3    Carlsen, S.4    Grubb, A.5
  • 6
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., Davis G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, G.2
  • 7
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A., Grzesiek S. Methodological advances in protein NMR. Accts. Chem. Res. 26:1993;131-138.
    • (1993) Accts. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 8
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett M. J., Schlunegger M. P., Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4:1995;2455-2468.
    • (1995) Protein Sci , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 9
    • 0024066065 scopus 로고
    • The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J., Kos J., Turk V. The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7:1988;2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 10
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G., Ruben D. J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Letters. 69:1980;185-189.
    • (1980) Chem. Phys. Letters , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 11
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning inEscherichia coli
    • Casadaban M. J., Cohen S. H. Analysis of gene control signals by DNA fusion and cloning inEscherichia coli. J. Mol. Biol. 138:1980;179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.H.2
  • 13
    • 0002974615 scopus 로고
    • New maximum entropy processing algorithm, with applications to nuclear magnetic resonance experiments
    • J. Skilling. Amsterdam: Kluwer Academic
    • Delsuc M. A. New maximum entropy processing algorithm, with applications to nuclear magnetic resonance experiments. Skilling J. Maximum Entropy and Bayesian Methods. 1989;Kluwer Academic, Amsterdam.
    • (1989) Maximum Entropy and Bayesian Methods
    • Delsuc, M.A.1
  • 14
  • 15
    • 0030052426 scopus 로고    scopus 로고
    • Folding-related dimerization of human cystatin C
    • Ekiel I., Abrahamson M. Folding-related dimerization of human cystatin C. J. Biol. Chem. 271:1996;1314-1321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1314-1321
    • Ekiel, I.1    Abrahamson, M.2
  • 16
    • 0027768859 scopus 로고
    • Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy
    • Engh R. A., Dieckmann T., Bode W., Auerswald E. A., Turk V., Huber R., Oschkinat H. Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy. J. Mol. Biol. 234:1993;1060-1069.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1060-1069
    • Engh, R.A.1    Dieckmann, T.2    Bode, W.3    Auerswald, E.A.4    Turk, V.5    Huber, R.6    Oschkinat, H.7
  • 19
    • 0011766298 scopus 로고
    • Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of γ-trace basic protein (cystatin C)
    • Ghiso J., Jensson O., Frangione B. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of γ-trace basic protein (cystatin C). Proc Natl. Acad. Sci. USA. 83:1986;2974-2978.
    • (1986) Proc Natl. Acad. Sci. USA , vol.83 , pp. 2974-2978
    • Ghiso, J.1    Jensson, O.2    Frangione, B.3
  • 20
    • 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. 114:1992;6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 22
    • 0026915084 scopus 로고
    • Cystatin-like cysteine proteinase inhibitors of parasitic protozoa
    • Irvine J. W., Coombs G. H., North M. J. Cystatin-like cysteine proteinase inhibitors of parasitic protozoa. FEMS Microbiol. Letters. 96:1992;67-72.
    • (1992) FEMS Microbiol. Letters , vol.96 , pp. 67-72
    • Irvine, J.W.1    Coombs, G.H.2    North, M.J.3
  • 26
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation
    • Kelly J. W., Lansbury P. T. A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation. Amyloid: Int. J. Expt. Clin. Invest. 1:1994;186-205.
    • (1994) Amyloid: Int. J. Expt. Clin. Invest. , vol.1 , pp. 186-205
    • Kelly, J.W.1    Lansbury, P.T.2
  • 27
    • 20444481878 scopus 로고    scopus 로고
    • Optimized adiabatic pulses for wideband spin inversion
    • Kupce, Freeman. Optimized adiabatic pulses for wideband spin inversion. J. Magn. Reson. Ser. A, 118:1996;299-303.
    • (1996) J. Magn. Reson. Ser. A , vol.118 , pp. 299-303
    • Kupce, F.1
  • 28
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure
    • Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins: Struct. Funct. Genet. 6:1989;87-103.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 29
    • 0024284781 scopus 로고
    • NMR sequential assignment ofEscherichia coli
    • LeMaster D. M., Richards F. M. NMR sequential assignment ofEscherichia coli. Biochemistry. 27:1988;142-150.
    • (1988) Biochemistry , vol.27 , pp. 142-150
    • LeMaster, D.M.1    Richards, F.M.2
  • 30
    • 33947473108 scopus 로고
    • The mutual diffusion of light and heavy water
    • Longsworth L. G. The mutual diffusion of light and heavy water. J. Phys. Chem. 64:1960;1914-1917.
    • (1960) J. Phys. Chem. , vol.64 , pp. 1914-1917
    • Longsworth, L.G.1
  • 32
    • 0028077339 scopus 로고
    • Structural characterization of human stefin A in solution and implications for binding to cysteine proteinases
    • Martin J. R., Jerala R., Kroon-Zitko L., Zerovnik E., Turk V., Waltho J. P. Structural characterization of human stefin A in solution and implications for binding to cysteine proteinases. Eur. J. Biochem. 225:1994;1181-1194.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 1181-1194
    • Martin, J.R.1    Jerala, R.2    Kroon-Zitko, L.3    Zerovnik, E.4    Turk, V.5    Waltho, J.P.6
  • 34
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore D. C., McIntosh L. P., Russell C. B., Anderson D. E., Dahlquist F. W. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177:1989;44-73.
    • (1989) Methods Enzymol. , vol.177 , pp. 44-73
    • Muchmore, D.C.1    McIntosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 36
    • 0025157221 scopus 로고
    • The amino terminal portion of cerebrospinal fluid cystatin C in hereditary cystatin C amyloid angiopathy is not truncated: Direct sequence analysis from agarose gel electropherograms
    • Olafsson I., Gudmundsson G., Abrahamson M., Jensson O., Grubb A. The amino terminal portion of cerebrospinal fluid cystatin C in hereditary cystatin C amyloid angiopathy is not truncated: direct sequence analysis from agarose gel electropherograms. Scand. J. Clin. Lab. Invest. 50:1990;85-93.
    • (1990) Scand. J. Clin. Lab. Invest. , vol.50 , pp. 85-93
    • Olafsson, I.1    Gudmundsson, G.2    Abrahamson, M.3    Jensson, O.4    Grubb, A.5
  • 38
    • 0026951903 scopus 로고
    • Gradient-taylored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-taylored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 40
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echoes in the presence of a time-dependent field gradient
    • Stejskal E. O., Tanner J. E. Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient. J. Chem. Phys. 42:1965;288-292.
    • (1965) J. Chem. Phys. , vol.42 , pp. 288-292
    • Stejskal, E.O.1    Tanner, J.E.2
  • 42
    • 0025301658 scopus 로고
    • The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs M. T., Laber B., Bode W., Huber R., Jerala R., Lenarcic, Turk V. The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J. 9:1990;1939-1990.
    • (1990) EMBO J. , vol.9 , pp. 1939-1990
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic6    Turk, V.7
  • 43
    • 0018339645 scopus 로고
    • The translational friction coefficient of proteins
    • Teller D. C., Swanson E., de Haën C. The translational friction coefficient of proteins. Methods Enzymol. 61:1979;103-124.
    • (1979) Methods Enzymol. , vol.61 , pp. 103-124
    • Teller, D.C.1    Swanson, E.2    De Haën, C.3
  • 44
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart D. S., Sykes B. D. Chemical shifts as a tool for structure determination. Methods Enzymol. 239:1994;363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 45
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind M., Mueller L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson. ser. B. 101:1993;201-205.
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.