메뉴 건너뛰기




Volumn 78, Issue 7, 1996, Pages 624-631

Conformational flexibility of tRNA: Structural changes in yeast tRNA(Asp) upon binding to aspartyl-tRNA synthetase

Author keywords

Aspartyl tRNA synthetase; Conformation; Transfer RNA

Indexed keywords

TRANSFER RNA;

EID: 0029906943     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(96)80008-3     Document Type: Article
Times cited : (21)

References (27)
  • 1
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 347:1990;203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 3
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase
    • Cusack S, Berthet-Colominas C, Härtlein M, Nassar N, Leberman R. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase. Nature. 347:1990;249-255.
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Härtlein, M.3    Nassar, N.4    Leberman, R.5
  • 4
    • 0027674975 scopus 로고
    • The aminoacyl-tRNA synthetase family: Modules at work
    • Delarue M, Moras D. The aminoacyl-tRNA synthetase family: modules at work. Bioessays. 15:1993;675-687.
    • (1993) Bioessays , vol.15 , pp. 675-687
    • Delarue, M.1    Moras, D.2
  • 10
    • 0025815046 scopus 로고
    • The 3 Å crystal structure of yeast initiator tRNA: Functional implications in initiator/elongator discrimination
    • Basavappa R, Sigler PB. The 3 Å crystal structure of yeast initiator tRNA: functional implications in initiator/elongator discrimination. EMBO J. 10:1991;3105-3111.
    • (1991) EMBO J , vol.10 , pp. 3105-3111
    • Basavappa, R.1    Sigler, P.B.2
  • 14
    • 0021879256 scopus 로고
    • Crystallographic refinement of yeast aspartic acid transfer RNA
    • Westhof E, Dumas P, Moras D. Crystallographic refinement of yeast aspartic acid transfer RNA. J Mol Biol. 184:1985;119-145.
    • (1985) J Mol Biol , vol.184 , pp. 119-145
    • Westhof, E.1    Dumas, P.2    Moras, D.3
  • 19
    • 0018077590 scopus 로고
    • Crystal structure of yeast phenylalanine transfer RNA. I. Crystallographic refinement
    • Sussmann JL, Holbrook SR, Warrant RW, Church GM, Kim SH. Crystal structure of yeast phenylalanine transfer RNA. I. Crystallographic refinement. J Mol Biol. 123:1978;607-630.
    • (1978) J Mol Biol , vol.123 , pp. 607-630
    • Sussmann, J.L.1    Holbrook, S.R.2    Warrant, R.W.3    Church, G.M.4    Kim, S.H.5
  • 20
    • 0017055057 scopus 로고
    • Crystallographic refinement of yeast phenylalanine transfer RNA at 2.5 Å resolution
    • Jack A, Ladner JE, Klug A. Crystallographic refinement of yeast phenylalanine transfer RNA at 2.5 Å resolution. J Mol Biol. 108:1976;619-649.
    • (1976) J Mol Biol , vol.108 , pp. 619-649
    • Jack, A.1    Ladner, J.E.2    Klug, A.3
  • 23
    • 0021891233 scopus 로고
    • Asp tertiary structure in solution and areas of interaction of the tRNA with aspartyl-tRNA synthetase. A comparative study of the yeast phenylalanine system by phosphate alkylation experiments with ethylnitrosourea
    • Asp tertiary structure in solution and areas of interaction of the tRNA with aspartyl-tRNA synthetase. A comparative study of the yeast phenylalanine system by phosphate alkylation experiments with ethylnitrosourea. J Mol Biol. 184:1985;455-471.
    • (1985) J Mol Biol , vol.184 , pp. 455-471
    • Romby, P.1    Moras, D.2    Bergdoll, M.3    Dumas, P.4    Vlassov, V.V.5    Westhof, E.6    Ebel, J.P.7    Giegé, R.8
  • 24
    • 0027129780 scopus 로고
    • Asp anticodon region with aspartyl-tRNA synthetase
    • Asp anticodon region with aspartyl-tRNA synthetase. BBRC. 186:1992;956-962.
    • (1992) BBRC , vol.186 , pp. 956-962
    • Garcia, A.1    Giegé, R.2
  • 26
    • 0025151612 scopus 로고
    • Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding
    • Bhat TN, Bentley GA, Fischmann TO, Boulot G, Poljak RJ. Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding. Nature. 347:1990;483-485.
    • (1990) Nature , vol.347 , pp. 483-485
    • Bhat, T.N.1    Bentley, G.A.2    Fischmann, T.O.3    Boulot, G.4    Poljak, R.J.5
  • 27
    • 0030047926 scopus 로고    scopus 로고
    • Refined structure of the monoclonal antibody HyHEL-5 with its antigen hen egg-white lysozyme
    • Cohen GH, Sheriff S, Davies DR. Refined structure of the monoclonal antibody HyHEL-5 with its antigen hen egg-white lysozyme. Acta Crystallogr. D52:1996;315-326.
    • (1996) Acta Crystallogr , vol.52 , pp. 315-326
    • Cohen, G.H.1    Sheriff, S.2    Davies, D.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.