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Volumn 4, Issue 9, 1997, Pages 751-759

Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA recognition by a protein containing a Zn2Cys6 binuclear cluster

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; TRANSCRIPTION FACTOR;

EID: 0030831985     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0997-751     Document Type: Article
Times cited : (89)

References (62)
  • 1
    • 0025968768 scopus 로고
    • Proline independent binding of PUT3 transcriptional activator protein detected by footprinting in vivo
    • Axelrod, J.D., Majors, J. & Brandriss, M.C. Proline independent binding of PUT3 transcriptional activator protein detected by footprinting in vivo. Mol. Cell. Biol. 11, 564-567(1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 564-567
    • Axelrod, J.D.1    Majors, J.2    Brandriss, M.C.3
  • 2
    • 0026315965 scopus 로고
    • Analysis of constitutive and noninducible mutations of the PUT3 transcriptional activator
    • Marczak, J.E. & Brandriss, M.C. Analysis of constitutive and noninducible mutations of the PUT3 transcriptional activator Mol. Cell. Biol. 11, 2609-2619 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2609-2619
    • Marczak, J.E.1    Brandriss, M.C.2
  • 3
    • 0024367337 scopus 로고
    • The Saccharomyces cerevisiae PUT3 activator protein associates with prolrne specific upstream activator sequences
    • Siddiqui, A.M. & Brandriss, M.C. The Saccharomyces cerevisiae PUT3 activator protein associates with prolrne specific upstream activator sequences. Mol. Cell. Biol. 9, 4706-4712 (1989).
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4706-4712
    • Siddiqui, A.M.1    Brandriss, M.C.2
  • 4
    • 0023443765 scopus 로고
    • Evidence for positive regulation of the proline utilization pathway in Saetbaromyces cerevisiae
    • Brandriss, M.C. Evidence for positive regulation of the proline utilization pathway in Saetbaromyces cerevisiae. Genetics 117, 429-435 (1987).
    • (1987) Genetics , vol.117 , pp. 429-435
    • Brandriss, M.C.1
  • 5
    • 0018637069 scopus 로고
    • Genetics and physiology of proline utilization in Saccharomyces cerevisiae: Mutation causing constitutive enzyme expression
    • Brandriss, M.C. & Magasanik, B. Genetics and physiology of proline utilization in Saccharomyces cerevisiae: mutation causing constitutive enzyme expression. J. Bacteriol. 140, 504-507 (1979).
    • (1979) J. Bacteriol. , vol.140 , pp. 504-507
    • Brandriss, M.C.1    Magasanik, B.2
  • 6
    • 0029803121 scopus 로고    scopus 로고
    • 6 zinc cluster family of transcriptional regulators
    • 6 zinc cluster family of transcriptional regulators. Nucleic Acids Res. 24, 4599-4607 (1996).
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4599-4607
    • Schjerling, P.1    Holmberg, S.2
  • 8
    • 0023493883 scopus 로고
    • A model fungal gene regulatory mechanism: The GAL genes of Saccharomyces cerevisiae
    • Johnston, M. A model fungal gene regulatory mechanism: the GAL genes of Saccharomyces cerevisiae Microbiol. Rev. 51, 458-476 (1987).
    • (1987) Microbiol Rev. , vol.51 , pp. 458-476
    • Johnston, M.1
  • 11
    • 0026547747 scopus 로고
    • DNA recognition by GAL4; structure of a protein-DNA complex
    • Marmorstein, R., Carey, M., Ptashne, M. & Harrison, S.C. DNA recognition by GAL4; structure of a protein-DNA complex. Nature 356, 408-414 (1992).
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 12
  • 13
    • 0026047966 scopus 로고
    • Refined crystal structure of Cd, Zn metallothionein at 2.0 A resolution
    • Robbins, A.H., et al. Refined crystal structure of Cd, Zn metallothionein at 2.0 A resolution. J. Mol. Biol. 221,1269-1293 (1991).
    • (1991) J. Mol. Biol. , vol.221 , pp. 1269-1293
    • Robbins, A.H.1
  • 14
    • 0023645234 scopus 로고
    • Metal co-ordination in rat liver metallothionein-2 prepared with and without reconstitution of the metal clusters, and comparison with rabbit liver metallothionein-2
    • Vasak, M., Worgotter, E., Wagner, G., Kagi, J.H. & Wuthrich, K. Metal co-ordination in rat liver metallothionein-2 prepared with and without reconstitution of the metal clusters, and comparison with rabbit liver metallothionein-2. J. Mol. Biol. 196, 711-719 (1987).
    • (1987) J. Mol. Biol. , vol.196 , pp. 711-719
    • Vasak, M.1    Worgotter, E.2    Wagner, G.3    Kagi, J.H.4    Wuthrich, K.5
  • 16
    • 0026582055 scopus 로고
    • Structure of the DNA binding domain of zinc GAL4
    • Kraulis, P.J., Raine, A.R.C, Gadhavi, P.L. & Laue, E.D. Structure of the DNA binding domain of zinc GAL4. Nature 356, 448-450 (1992).
    • (1992) Nature , vol.356 , pp. 448-450
    • Kraulis, P.J.1    Raine, A.R.C.2    Gadhavi, P.L.3    Laue, E.D.4
  • 17
    • 0030596420 scopus 로고    scopus 로고
    • 15N Resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain
    • 15N Resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain. J. Mol. Biol. 259, 792-804 (1996).
    • (1996) J. Mol. Biol. , vol.259 , pp. 792-804
    • Timmerman, J.1
  • 19
    • 0025272940 scopus 로고
    • Alpha-helical coiled coils and bundles: How to design an alphahelical protein
    • Cohen, C & Parry, D.A. Alpha-helical coiled coils and bundles: how to design an alphahelical protein. Proteins 7, 1-15 (1990).
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.2
  • 20
    • 0024295767 scopus 로고
    • The leucine zipper; a hypothetical structure common to a new class of DNA binding proteins
    • Landschultz, W.H., Johnson, P.F & Mcknight, S.L The leucine zipper; a hypothetical structure common to a new class of DNA binding proteins. Science 245, 1759-1764 (1988).
    • (1988) Science , vol.245 , pp. 1759-1764
    • Landschultz, W.H.1    Johnson, P.F.2    Mcknight, S.L.3
  • 21
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two stranded parallel coiled-coil
    • O'Shea, E.X., Klemm, J.D., Kim, P.S. & Alber, T. X-ray structure of the GCN4 leucine zipper, a two stranded parallel coiled-coil. Science 254, 539-544 (1991).
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.X.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 22
    • 0024554495 scopus 로고
    • A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, myoD, and myc proteins
    • Murre, C, McCaw, P.S. & Baltimore, D. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, myoD, and myc proteins. Cell 56, 777-783 (1989).
    • (1989) Cell , vol.56 , pp. 777-783
    • Murre, C.1    McCaw, P.S.2    Baltimore, D.3
  • 23
    • 0025253013 scopus 로고
    • Transcriptional regulation by dimerization: Two sides to an incestuous relationship
    • Jones, N, Transcriptional regulation by dimerization: two sides to an incestuous relationship. Cell 61, 9-11 (1990).
    • (1990) Cell , vol.61 , pp. 9-11
    • Jones, N.1
  • 24
    • 0029075461 scopus 로고
    • Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner, M.H., Huth, J.R., Gronenborn, A.M. & Clore, G.M. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell 81, 705-714 (1995).
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 25
    • 0029131298 scopus 로고
    • Et al Structural basis for DNA bending by architectural transcription factor LEM
    • Love, J.J., et al Structural basis for DNA bending by architectural transcription factor LEM. Nature 376, 791-795 (1995).
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1
  • 26
    • 0028173030 scopus 로고
    • Crystal structure of Lad member, PurR, bound to DNA: Minor groove binding by a helices
    • Schumacher, M,A., Choi, K.Y., Zalkin, H. & Brennan, R.G. Crystal structure of Lad member, PurR, bound to DNA: minor groove binding by a helices. Science 266, 763-770 (1994).
    • (1994) Science , vol.266 , pp. 763-770
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennan, R.G.4
  • 27
    • 0029938053 scopus 로고    scopus 로고
    • Crystal structure of the lactose operon represser and its complexes with DNA and inducer
    • Lewis, M., et al. Crystal structure of the lactose operon represser and its complexes with DNA and inducer.Science 271,1247-1254 (1996).
    • (1996) Science , vol.271 , pp. 1247-1254
    • Lewis, M.1
  • 28
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim, J.L., Nikolov, D.B. & Burley, S.K. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365, 520-527 (1993).
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 29
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kirn, Y., Geiger, J.H., Hahn, S. & Sigler, P.B. Crystal structure of a yeast TBP/TATA-box complex. Nature 365, 512-520 (1993).
    • (1993) Nature , vol.365 , pp. 512-520
    • Kirn, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 30
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of a IHF-DNA complex: A protein-induced DNA U-turn
    • Rice, P.A., Yang, S.-W., Mizuuchi, K. & Nash, H.A. Crystal structure of a IHF-DNA complex: a protein-induced DNA U-turn, Cell 87, 1295-1306 (1996).
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.-W.2    Mizuuchi, K.3    Nash, H.A.4
  • 31
    • 0030046809 scopus 로고    scopus 로고
    • Intercalation, DNA kinking, and control of transcription
    • Werner, M,H., Gronenborn, A.M. & Clore, G.M. Intercalation, DNA kinking, and control of transcription. Science 271, 778-784 (1996).
    • (1996) Science , vol.271 , pp. 778-784
    • Werner, M.H.1    Gronenborn, A.M.2    Clore, G.M.3
  • 32
    • 1842360636 scopus 로고    scopus 로고
    • Studies on the half-site spacing specificity of the yeast zinc cluster protein PUT3
    • in the press
    • Hoff man, P. & Schepartz, A. Studies on the half-site spacing specificity of the yeast zinc cluster protein PUT3. Bio. Med. Chern. Lett., in the press.
    • Bio. Med. Chern. Lett.
    • Hoff Man, P.1    Schepartz, A.2
  • 33
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90°
    • Schultz, S.C., Shields, G.C. & Steitz, T.A. Crystal structure of a CAP-DNA complex: the DNA is bent by 90°.Science 253, 1001-1007 (1991).
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 34
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • Hegde, R.S., Grossman, S.R., Laimins, L.A. & Sigler, PB. Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target Nature 359, 505-512 (1992).
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 35
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZIP bound to a ATF/CREB site DNA shows the complex depends on DNA flexibility
    • Konig, P. & Richmond, T.J. The X-ray structure of the GCN4-bZIP bound to a ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol. 233, 139-154 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 139-154
    • Konig, P.1    Richmond, T.J.2
  • 36
    • 0029563634 scopus 로고
    • Crystal structure of a bZIP/DNA complex at 2.2 A: Determinants of DNA specific recognition
    • Keller, W., Konig, P. & Richmond, T.J. Crystal structure of a bZIP/DNA complex at 2.2 A: determinants of DNA specific recognition. J. Mol. Biol. 254, 657-667 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 657-667
    • Keller, W.1    Konig, P.2    Richmond, T.J.3
  • 37
    • 0027049805 scopus 로고
    • The GCN4 basic-region leucine zipper binds DNA as a dimer of uninterrupted a-helices: Crystal structure of the protein-DNA complex
    • Ellenberger, T.E., Brandi, C.J., Struhl, K. & Harrison, S.C. The GCN4 basic-region leucine zipper binds DNA as a dimer of uninterrupted a-helices: crystal structure of the protein-DNA complex. Cell 71,1223-1237. (1992).
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandi, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 38
    • 0025155512 scopus 로고
    • Folding transitions in the DNA-binding domain of GCN4 on specific binding to DNA
    • Weiss, M.A., et al Folding transitions in the DNA-binding domain of GCN4 on specific binding to DNA. Nature 347, 575-578 (1990).
    • (1990) Nature , vol.347 , pp. 575-578
    • Weiss, M.A.1
  • 39
    • 0025991706 scopus 로고
    • DNA-induced increase in the ahelical content of QEBP and GCN4
    • O'Neil, K.T., Shuman, J-D., Ampe, C. & Degrado, W.F. DNA-induced increase in the ahelical content of QEBP and GCN4. Biochemistry 30, 9030-9034 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9030-9034
    • O'Neil, K.T.1    Shuman, J.-D.2    Ampe, C.3    Degrado, W.F.4
  • 40
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R.S.& Record, M.T. Coupling of local folding to site-specific binding of proteins to DNA. Science 263, 777-784 (1994).
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 41
    • 0026069207 scopus 로고
    • LAC9 DNA binding domain coordinates two zinc atoms per monomer and contacts DNA as a dimer
    • Halvorsen, Y.-D.C, Nandabalan, K. & Dickson, P.C. LAC9 DNA binding domain coordinates two zinc atoms per monomer and contacts DNA as a dimer Mol. Cell. Biol. 11, 1777-1784 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1777-1784
    • Halvorsen, Y.-D.C.1    Nandabalan, K.2    Dickson, P.C.3
  • 42
    • 0023131381 scopus 로고
    • Characterization of a positive regulatory gene, LAC9, that controls induction of the lactose-galactose regulone of Kluyveromyces lactis: Structural and functional relationships to GAL4 of Saccharomyces cerevisiae
    • Wray, LUJ., Witte, M.M., Dickson, R.C. & Riley, M.I. Characterization of a positive regulatory gene, LAC9, that controls induction of the lactose-galactose regulone of Kluyveromyces lactis: structural and functional relationships to GAL4 of Saccharomyces cerevisiae. Mol. Cell. Biol. 7, 1111-1121 (1987).
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1111-1121
    • Wray, L.1    Witte, M.M.2    Dickson, R.C.3    Riley, M.I.4
  • 43
    • 0021829055 scopus 로고
    • Gene organization and regulation intheqa (quinic acid) gene cluster of Neurospora crassa
    • Giles, N.M., et al. Gene organization and regulation intheqa (quinic acid) gene cluster of Neurospora crassa. Microbiol Rev., 338-358 (1985).
    • (1985) Microbiol Rev. , pp. 338-358
    • Giles, N.M.1
  • 44
    • 0021340875 scopus 로고
    • Molecular analysis of the Neurospora qa-1 regulatory region indicates that two interacting genes control qa gene expression
    • Huit, L. Molecular analysis of the Neurospora qa-1 regulatory region indicates that two interacting genes control qa gene expression. Proc. Natl. Acad. Sci. USA 81, 1174-1178 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1174-1178
    • Huit, L.1
  • 45
    • 0005902156 scopus 로고
    • Genetic organization and transcriptional regulation intheqa gene cluster of Neurospora crassa
    • Patel, V.B., Schweizer, M., Dykstra, C.C., Kushner, S.R. & Giles, N,H. Genetic organization and transcriptional regulation intheqa gene cluster of Neurospora crassa. Proc. Natl Acad. Sci. USA 78, 5783-5787 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 5783-5787
    • Patel, V.B.1    Schweizer, M.2    Dykstra, C.C.3    Kushner, S.R.4    Giles, N.H.5
  • 46
    • 0027218382 scopus 로고
    • Determinants of binding site specificity among yeast C6 zinc clusterproteins
    • Reece, R.J. & Ptashne, M. Determinants of binding site specificity among yeast C6 zinc clusterproteins. Science 261, 909-911 (1993).
    • (1993) Science , vol.261 , pp. 909-911
    • Reece, R.J.1    Ptashne, M.2
  • 47
    • 0029802537 scopus 로고    scopus 로고
    • A novel DNA binding motif for yeast zinc cluster proteins: The LeuBp and Pdr3p transcriptional activators recognize everted repeats
    • Hellauer, K., Rochon, M.H. & Turcotte, B. A novel DNA binding motif for yeast zinc cluster proteins: the LeuBp and Pdr3p transcriptional activators recognize everted repeats. Mol. Cell. Biol. 16, 6096-6102 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6096-6102
    • Hellauer, K.1    Rochon, M.H.2    Turcotte, B.3
  • 48
    • 0028071873 scopus 로고
    • The yeast activator HAP1 - A GAL4 family member-binds DNA in a directly repeated orientation
    • Zhang, L&Guarente, L. The yeast activator HAP1 - a GAL4 family member-binds DNA in a directly repeated orientation. Genes Dev. 8, 2110-2119 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 2110-2119
    • Zhang, L.1    Guarente, L.2
  • 49
    • 0029811436 scopus 로고    scopus 로고
    • The C6 zinc cluster dictates asymmetric binding by HAP1
    • Zhang, L. & Guarente, L The C6 zinc cluster dictates asymmetric binding by HAP1, EMBOJ. 15, 4676-4681 (1996).
    • (1996) EMBOJ. , vol.15 , pp. 4676-4681
    • Zhang, L.1    Guarente, L.2
  • 50
    • 44949289693 scopus 로고
    • Crystallization of DNA binding proteins with oligonucleotides
    • Aggarwal, A.K. Crystallization of DNA binding proteins with oligonucleotides. Methods: A companion to Methods in Enzymology 1, 83-90 (1990).
    • (1990) Methods: a Companion to Methods in Enzymology , vol.1 , pp. 83-90
    • Aggarwal, A.K.1
  • 51
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch, W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 21, 67-71 (1988).
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 67-71
    • Kabsch, W.1
  • 52
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21, 916-924 (1988).
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 54
    • 0011975439 scopus 로고
    • PHASES: A program package for the processing and analysis of diffraction data from macromolecules
    • eds. Carter, C. & Sweet, R. (Academic Press, Qrlando, FL)
    • Furey, W. & Swaminathan, S. PHASES: A program package for the processing and analysis of diffraction data from macromolecules. in Meth. Enzymology (eds. Carter, C. & Sweet, R.) (Academic Press, Qrlando, FL, 1995).
    • (1995) Meth. Enzymology
    • Furey, W.1    Swaminathan, S.2
  • 55
    • 0000356656 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. Crystallogr. 11, 268-272 (1978).
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 56
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity assessing the accuracy of crystal structures
    • Brunger, A.T. The free R value: a novel statistical quantity assessing the accuracy of crystal structures. Nature 335, 472-174 (1992).
    • (1992) Nature , vol.335 , pp. 472-1174
    • Brunger, A.T.1
  • 58
    • 0023140814 scopus 로고
    • Cristallographie R factor refinement by molecular dynamics
    • Brunger, A.T., Kuriyan, J. & Karplus, M. Cristallographie R factor refinement by molecular dynamics. Science 235, 458-460 (1987).
    • (1987) Science , vol.235 , pp. 458-460
    • Brunger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 59
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystal structures
    • Model, A., Kim, S.-H. & Brunger, A.T. Model bias in macromolecular crystal structures, Acta. Crystallogr. A48, 851-858 (1992).
    • (1992) Acta. Crystallogr. , vol.A48 , pp. 851-858
    • Model, A.1    Kim, S.-H.2    Brunger, A.T.3
  • 61
    • 0028057108 scopus 로고
    • RASTER3D version 2.0: A program for photorealistic molecular graphics
    • Merritt, E,A. & Murphy, M.E.P. RASTER3D version 2.0: a program for photorealistic molecular graphics.Acta Crystallogr. D50, 869-873 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 62
    • 0026244229 scopus 로고
    • MOLSCRIPT; A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT; A program to produce both detailed and schematic plots of protein structures. J, Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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