메뉴 건너뛰기




Volumn 5, Issue 2, 1998, Pages 133-139

Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; RNA;

EID: 0031951789     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0298-133     Document Type: Review
Times cited : (122)

References (45)
  • 1
    • 0031563817 scopus 로고    scopus 로고
    • Structure, recognition and adaptive binding in RNA aptamer complexes
    • Patel, D.J. et al. Structure, recognition and adaptive binding in RNA aptamer complexes. J. Mol. Biol. 272, 645-664 (1997).
    • (1997) J. Mol. Biol. , vol.272 , pp. 645-664
    • Patel, D.J.1
  • 2
    • 0030475417 scopus 로고    scopus 로고
    • Deep penetration of an & alpha;-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex
    • Ye, X., Gorin, A., Ellington, A.D. & Patel, D.J. Deep penetration of an & alpha;-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex. Nature Struct. Biol. 3, 1026-1033 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1026-1033
    • Ye, X.1    Gorin, A.2    Ellington, A.D.3    Patel, D.J.4
  • 3
    • 0027104297 scopus 로고
    • Selection of high affinity RNA figands to the bacteriophage R17 coat protein
    • Schneider, D., Tuerk, C. & Gold, L Selection of high affinity RNA figands to the bacteriophage R17 coat protein. J. Mol. Biol. 228, 862-869 (1992).
    • (1992) J. Mol. Biol. , vol.228 , pp. 862-869
    • Schneider, D.1    Tuerk, C.2    Gold, L.3
  • 4
    • 0029062420 scopus 로고
    • In vitro selection of RNA ligands to substance-P
    • Nieuwlandt, D., Wecker, M. & Gold, L. In vitro selection of RNA ligands to substance-P. Biochemistry 34, 5651-5659 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5651-5659
    • Nieuwlandt, D.1    Wecker, M.2    Gold, L.3
  • 5
    • 0027173323 scopus 로고
    • 3 small ribooligonucleotides with specificarginine sites
    • Connell, G.J., Ulangesekare, M. & Yarus, M. 3 small ribooligonucleotides with specificarginine sites. Biochemistry 32, 5497-5502 (1993).
    • (1993) Biochemistry , vol.32 , pp. 5497-5502
    • Connell, G.J.1    Ulangesekare, M.2    Yarus, M.3
  • 6
    • 0027180473 scopus 로고
    • An RNA motif that binds ATP
    • Sassanfar, M. & Szostak, J.W. An RNA motif that binds ATP. Nature 364, 550-555 (1993).
    • (1993) Nature , vol.364 , pp. 550-555
    • Sassanfar, M.1    Szostak, J.W.2
  • 7
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington, A.D. & Szostak, J.W. In vitro selection of RNA molecules that bind specific ligands. Nature 346, 818-822 (1990).
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 8
    • 0028224199 scopus 로고
    • High resolution molecular discrimination by RNA
    • Jenison, R.D., Gill, S., Pardi, A. & Polisky, B. High resolution molecular discrimination by RNA. Science 263, 1425-1429 (1994).
    • (1994) Science , vol.263 , pp. 1425-1429
    • Jenison, R.D.1    Gill, S.2    Pardi, A.3    Polisky, B.4
  • 9
    • 0001878781 scopus 로고
    • eds. Gesteland, R.F. & Atkins, J.F. (Cold Spring Harbor Press, New York)
    • Szostah,J.M. & Ellington, A.D. In The RNA world (eds. Gesteland, R.F. & Atkins, J.F.) 511-534 (Cold Spring Harbor Press, New York; 1993).
    • (1993) The RNA World , pp. 511-534
    • Szostah, J.M.1    Ellington, A.D.2
  • 10
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Valegård, K., Murray, J.B., Stockley, P.G., Stonehouse, N.J. & Liljas, L. Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371, 623-626 (1994).
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegård, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouse, N.J.4    Liljas, L.5
  • 11
    • 0031213649 scopus 로고    scopus 로고
    • The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions
    • Valegård, K. et al. The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions. J. Mol. Biol. 270, 724-738 (1997).
    • (1997) J. Mol. Biol. , vol.270 , pp. 724-738
    • Valegård, K.1
  • 12
    • 0025982691 scopus 로고
    • Specific interaction between RNA phage coat protein and RNA
    • Witherell, G.W., Gott, J.M. & Uhlenbeck, O.C. Specific interaction between RNA phage coat protein and RNA. Prog. Nuc. Acid Res. 40, 185-220 (1991).
    • (1991) Prog. Nuc. Acid Res. , vol.40 , pp. 185-220
    • Witherell, G.W.1    Gott, J.M.2    Uhlenbeck, O.C.3
  • 13
    • 0025300971 scopus 로고
    • Use of synthetic oligoribonucleotides to probe RNA-protein interactions in the MS2 translational operator complex
    • Tatbot, S.J., Goodman, S., Bates, S.R.E., Fishwick, C.W.G. & Stockley, P.C. Use of synthetic oligoribonucleotides to probe RNA-protein interactions in the MS2 translational operator complex. Nucleic Acids Res. 18, 3521-3528 (1990).
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3521-3528
    • Tatbot, S.J.1    Goodman, S.2    Bates, S.R.E.3    Fishwick, C.W.G.4    Stockley, P.C.5
  • 14
    • 0029053759 scopus 로고
    • Probing sequence-specific RNA recognition by the bacteriophage MS2 coat protein
    • Stockley, P.G. et al. Probing sequence-specific RNA recognition by the bacteriophage MS2 coat protein. Nucleic Acids Res. 23, 2512-2518 (1995).
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2512-2518
    • Stockley, P.G.1
  • 15
    • 0025344593 scopus 로고
    • The three-dimensional structure of the bacterial virus MS2 capsids
    • Valegård, K., Liljas, L., Fridborg, K. & Unge, T. The three-dimensional structure of the bacterial virus MS2 capsids. Nature 345, 36-41 (1990).
    • (1990) Nature , vol.345 , pp. 36-41
    • Valegård, K.1    Liljas, L.2    Fridborg, K.3    Unge, T.4
  • 16
    • 0027404265 scopus 로고
    • The RNA binding site of bacteriophage MS2 coat protein
    • Peabody, D.S. The RNA binding site of bacteriophage MS2 coat protein. EMBO J. 12, 595-600 (1993).
    • (1993) EMBO J. , vol.12 , pp. 595-600
    • Peabody, D.S.1
  • 17
    • 0028060580 scopus 로고
    • Mutations that increase the affinity of a translational represser for RNA
    • Lim, F. & Peabody, D.S. Mutations that increase the affinity of a translational represser for RNA. Nucleic Acids Res. 22, 3748-3752 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3748-3752
    • Lim, F.1    Peabody, D.S.2
  • 19
    • 0023597556 scopus 로고
    • An RNA mutation that increases the affinity of an RNA-protein interaction
    • Lowary, P.T. & Uhlenbeck, O.C. An RNA mutation that increases the affinity of an RNA-protein interaction. Nucleic Acids Res. 15, 10483-10493 (1987).
    • (1987) Nucleic Acids Res. , vol.15 , pp. 10483-10493
    • Lowary, P.T.1    Uhlenbeck, O.C.2
  • 20
    • 0029644408 scopus 로고
    • Crystal structure of the MS2 coat protein dimer: Implications for RNA binding and virus assembly
    • Ni, C.-Z. et al. Crystal structure of the MS2 coat protein dimer: implications for RNA binding and virus assembly. Structure 3, 255-263 (1995).
    • (1995) Structure , vol.3 , pp. 255-263
    • Ni, C.-Z.1
  • 21
    • 0030755831 scopus 로고    scopus 로고
    • MS2 coat protein mutants which bind Q β RNA
    • Spingola, M. & Peabody, D.S. MS2 coat protein mutants which bind Q β RNA. Nucleic Acids Res. 25, 2808-2815 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2808-2815
    • Spingola, M.1    Peabody, D.S.2
  • 22
    • 0028292548 scopus 로고
    • Altering the RNA binding specificity of a translational repressor
    • Lim, F., Spingola, M. & Peabody, D.S. Altering the RNA binding specificity of a translational repressor. J. Biol. Chem. 269, 9006-9010 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 9006-9010
    • Lim, F.1    Spingola, M.2    Peabody, D.S.3
  • 23
    • 0029731344 scopus 로고    scopus 로고
    • The RNA-binding site of bacteriophage Qβ coat protein
    • Lim, F., Spingola, M. & Peabody, D.S. The RNA-binding site of bacteriophage Qβ coat protein. J. Biol. Chem. 271, 31839-31845 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31839-31845
    • Lim, F.1    Spingola, M.2    Peabody, D.S.3
  • 24
    • 0024264659 scopus 로고
    • Ribonucleoprotein complexes of R17 coat protein and a translational operator analog
    • Beckett, D. & Uhlenbeck, O.C. Ribonucleoprotein complexes of R17 coat protein and a translational operator analog. J. Mol. Biol. 204, 927-938 (1988).
    • (1988) J. Mol. Biol. , vol.204 , pp. 927-938
    • Beckett, D.1    Uhlenbeck, O.C.2
  • 26
    • 0030831668 scopus 로고    scopus 로고
    • Mutant ATP-binding RNA aptamers reveal the structural basis for ligand binding
    • Dieckmann, T., Butcher, S.E., Sassanfar, M., Szostak, J.W. & Feigon, J. Mutant ATP-binding RNA aptamers reveal the structural basis for ligand binding. J. Mol Biol. 273, 467-478 (1997).
    • (1997) J. Mol Biol. , vol.273 , pp. 467-478
    • Dieckmann, T.1    Butcher, S.E.2    Sassanfar, M.3    Szostak, J.W.4    Feigon, J.5
  • 27
    • 0030761058 scopus 로고    scopus 로고
    • RNA structure comes of age
    • Uhlenbeck, O.C., Pardi, A. & Feigon, J. RNA structure comes of age. Cell 90, 833-840 ( 1997).
    • (1997) Cell , vol.90 , pp. 833-840
    • Uhlenbeck, O.C.1    Pardi, A.2    Feigon, J.3
  • 28
    • 0029099218 scopus 로고
    • 11 down and 9 to go
    • Cusack, S. 11 down and 9 to go. Nature Struct. Biol. 2, 824-831 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 824-831
    • Cusack, S.1
  • 29
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, N., Evans, P.R., Teo, C.-H. & Nagai, K. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Mature 372, 432-438 (1994).
    • (1994) Mature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.-H.4    Nagai, K.5
  • 30
    • 0027407913 scopus 로고
    • Multiple presentation of foreign peptides on the surface of an RNA-free spherical bacteriophage capsid
    • Masttco, R.A., Talbot, S.J. & Stockley, P.G. Multiple presentation of foreign peptides on the surface of an RNA-free spherical bacteriophage capsid. J. Gen. Virol. 74, 541-548 (1993).
    • (1993) J. Gen. Virol. , vol.74 , pp. 541-548
    • Masttco, R.A.1    Talbot, S.J.2    Stockley, P.G.3
  • 31
    • 0027508172 scopus 로고
    • Effects of amino acid substitution on the thermal stability of MS2 capsids lacking genomic RNA
    • Stonehouse, N.J. & Stockley, P.G. Effects of amino acid substitution on the thermal stability of MS2 capsids lacking genomic RNA. FEBS Letts. 334, 355-359 (1993).
    • (1993) FEBS Letts. , vol.334 , pp. 355-359
    • Stonehouse, N.J.1    Stockley, P.G.2
  • 32
    • 0023053744 scopus 로고
    • Purification, crystallization and preliminary X-ray data collection of the bacteriophage MS2
    • Valegård, K., Unge, T., Montelius, I., Strandberg, B. & Fiers W. Purification, crystallization and preliminary X-ray data collection of the bacteriophage MS2. J. Mol. Biol. 190, 587-591 (1986).
    • (1986) J. Mol. Biol. , vol.190 , pp. 587-591
    • Valegård, K.1    Unge, T.2    Montelius, I.3    Strandberg, B.4    Fiers, W.5
  • 33
    • 0028205651 scopus 로고
    • A general purification procedure for chemically synthesised oligoribonucleotides
    • Murray, J.B., Collier, A.K. & Arnold, J.R.P. A general purification procedure for chemically synthesised oligoribonucleotides. Anal. Biochem. 218, 177-184 (1994).
    • (1994) Anal. Biochem. , vol.218 , pp. 177-184
    • Murray, J.B.1    Collier, A.K.2    Arnold, J.R.P.3
  • 34
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4. the CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 35
    • 0027140498 scopus 로고
    • The refined structure of bacteriophage MS2 at 2.8 Å resolution
    • Golmohammadi, R., Valegård, K., Fridborg, K. & Liljas, L. The refined structure of bacteriophage MS2 at 2.8 Å resolution. J. Mol. Biol. 234, 620-639 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 620-639
    • Golmohammadi, R.1    Valegård, K.2    Fridborg, K.3    Liljas, L.4
  • 36
    • 0002700643 scopus 로고
    • eds Bailey, S., Hubbard, R. & Waller, D. (EPSRC Daresbury Laboratory, Warrington, UK)
    • Kleywegt, GJ. & Jones, T.A. In From first map to final model (eds Bailey, S., Hubbard, R. & Waller, D.) 59-66 (EPSRC Daresbury Laboratory, Warrington, UK; 1994).
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 38
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brũnger, AT., Kuriyan, J. & Karplus, M. Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460 (1987).
    • (1987) Science , vol.235 , pp. 458-460
    • Brũnger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 39
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A47, 392-400 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 41
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 42
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J.-S. & Brũnger, A.T. Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115 (1994).
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brũnger, A.T.2
  • 43
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol. Graphics 15, 133-138 (1997).
    • (1997) J Mol. Graphics , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 44
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units
    • Ramakrishnan, C. & Ramachandran, G.N. Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units. Biophys J. 5, 909-933 (1965).
    • (1965) Biophys J. , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.