메뉴 건너뛰기




Volumn 334, Issue 3, 2003, Pages 551-565

Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed

Author keywords

Chitin binding domain; Lectin; Pokeweed; Protein carbohydrate interaction; Protein protein interaction

Indexed keywords

AROMATIC COMPOUND; CARBOHYDRATE; CARBOHYDRATE BINDING PROTEIN; CHITIN; DIMER; LIGAND; PLANT LECTIN; POLYPEPTIDE; PROTEIN SUBUNIT; TRI N ACETYLCHITOTRIOSE; TRIOSE; TRISACCHARIDE; UNCLASSIFIED DRUG; WHEAT GERM AGGLUTININ;

EID: 0242493816     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.076     Document Type: Article
Times cited : (24)

References (62)
  • 1
    • 0022495827 scopus 로고
    • Cell-surface carbohydrates in cell recognition and response
    • Brandley B.K., Schnaar R.L. Cell-surface carbohydrates in cell recognition and response. J. Leukoc. Biol. 40:1986;97-111.
    • (1986) J. Leukoc. Biol. , vol.40 , pp. 97-111
    • Brandley, B.K.1    Schnaar, R.L.2
  • 2
    • 0023811955 scopus 로고
    • Transmembrane signals in the activation of T-lymphocytes by lectin mitogens
    • Hadden J.W. Transmembrane signals in the activation of T-lymphocytes by lectin mitogens. Mol. Immunol. 25:1988;1105-1112.
    • (1988) Mol. Immunol. , vol.25 , pp. 1105-1112
    • Hadden, J.W.1
  • 3
    • 0024742524 scopus 로고
    • Wheat-germ agglutinin induces mating reactions in Chlamydomonas eugametos by cross-linking agglutinin-associated glycoproteins in the flagellar membrane
    • Kooijman R., de Wildt P., Beumer S., van der Vliet G., Homan W., Kalshoven H., et al. Wheat-germ agglutinin induces mating reactions in Chlamydomonas eugametos by cross-linking agglutinin-associated glycoproteins in the flagellar membrane. J. Cell Biol. 109:1989;1677-1687.
    • (1989) J. Cell Biol. , vol.109 , pp. 1677-1687
    • Kooijman, R.1    De Wildt, P.2    Beumer, S.3    Van Der Vliet, G.4    Homan, W.5    Kalshoven, H.6
  • 4
    • 0024340857 scopus 로고
    • Role of carbohydrates in glycoprotein hormone signal transduction
    • Sairam M.R. Role of carbohydrates in glycoprotein hormone signal transduction. FASEB J. 3:1989;1915-1926.
    • (1989) FASEB J. , vol.3 , pp. 1915-1926
    • Sairam, M.R.1
  • 6
    • 0016234862 scopus 로고
    • Isolation, characterization, and biological activities of five mitogens from pokeweed
    • Waxdal M.J. Isolation, characterization, and biological activities of five mitogens from pokeweed. Biochemistry. 13:1974;3671-3677.
    • (1974) Biochemistry , vol.13 , pp. 3671-3677
    • Waxdal, M.J.1
  • 7
    • 0017097318 scopus 로고
    • The effects of purified mitogenic proteins (Pa-1 and Pa-2) from pokeweed on human T and B lymphocytes in vitro
    • Janossy G., Gomez De La Concha E., Waxdal M.J., Platts-Mills T. The effects of purified mitogenic proteins (Pa-1 and Pa-2) from pokeweed on human T and B lymphocytes in vitro. Clin. Expt. Immunol. 26:1976;108-117.
    • (1976) Clin. Expt. Immunol. , vol.26 , pp. 108-117
    • Janossy, G.1    Gomez De La Concha, E.2    Waxdal, M.J.3    Platts-Mills, T.4
  • 8
    • 0017260975 scopus 로고
    • Purification and biological activities of pokeweed (Phytolacca americana) mitogens
    • Yokoyama K., Yano O., Terao T., Osawa T. Purification and biological activities of pokeweed (Phytolacca americana) mitogens. Biochim. Biophys. Acta. 427:1976;443-452.
    • (1976) Biochim. Biophys. Acta , vol.427 , pp. 443-452
    • Yokoyama, K.1    Yano, O.2    Terao, T.3    Osawa, T.4
  • 9
    • 0023623217 scopus 로고
    • T cell mitogens and polyclonal B cell activators
    • Di Sabato G., Hall J.M., Thompson L. T cell mitogens and polyclonal B cell activators. Methods Enzymol. 150:1987;3-17.
    • (1987) Methods Enzymol. , vol.150 , pp. 3-17
    • Di Sabato, G.1    Hall, J.M.2    Thompson, L.3
  • 11
    • 85007816008 scopus 로고
    • Purification and characterization of three mitogenic lections from the roots of pokeweed (Phytolacca americana)
    • Kino M., Yamaguchi K., Umekawa H., Funatsu G. Purification and characterization of three mitogenic lections from the roots of pokeweed (Phytolacca americana). Biosci. Biotech. Biochem. 59:1995;683-688.
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 683-688
    • Kino, M.1    Yamaguchi, K.2    Umekawa, H.3    Funatsu, G.4
  • 12
    • 0029334938 scopus 로고
    • The complete amino acid sequence of lectin-C from the roots of pokeweed (Phytolacca americana)
    • Yamaguchi K., Mori A., Funatsu G. The complete amino acid sequence of lectin-C from the roots of pokeweed (Phytolacca americana). Biosci. Biotechnol. Biochem. 59:1995;1384-1385.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1384-1385
    • Yamaguchi, K.1    Mori, A.2    Funatsu, G.3
  • 13
    • 0030220520 scopus 로고    scopus 로고
    • Amino acid sequence and some properties of lectin-D from the roots of pokeweed (Phytolacca americana)
    • Yamaguchi K., Mori A., Funatsu G. Amino acid sequence and some properties of lectin-D from the roots of pokeweed (Phytolacca americana). Biosci. Biotechnol. Biochem. 60:1996;1380-1382.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1380-1382
    • Yamaguchi, K.1    Mori, A.2    Funatsu, G.3
  • 14
    • 0031126779 scopus 로고    scopus 로고
    • The amino acid seqence of mitogenic lectin-B from the roots of pokeweed (Phytolacca americana)
    • Yamaguchi K., Yurino N., Kino M., Ishiguro M., Funatsu G. The amino acid seqence of mitogenic lectin-B from the roots of pokeweed (Phytolacca americana). Biosci. Biotechnol. Biochem. 61:1997;690-698.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 690-698
    • Yamaguchi, K.1    Yurino, N.2    Kino, M.3    Ishiguro, M.4    Funatsu, G.5
  • 15
    • 0033593246 scopus 로고    scopus 로고
    • Crystal structure of a dimeric mannose-specific agglutinin from garlic: Quaternary association and carbohydrate specificity
    • Chandra N.R., Ramachandraiah G., Bachhawat K., Dam T.K., Surolia A., Vijayan M. Crystal structure of a dimeric mannose-specific agglutinin from garlic: quaternary association and carbohydrate specificity. J. Mol. Biol. 285:1999;1157-1168.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1157-1168
    • Chandra, N.R.1    Ramachandraiah, G.2    Bachhawat, K.3    Dam, T.K.4    Surolia, A.5    Vijayan, M.6
  • 16
    • 0034674159 scopus 로고    scopus 로고
    • The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: Crystal structure of cross-linked FRIL
    • Hamelryck T.W., Moore J.G., Chrispeels M.J., Loris R., Wyns L. The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL. J. Mol. Biol. 299:2000;875-883.
    • (2000) J. Mol. Biol. , vol.299 , pp. 875-883
    • Hamelryck, T.W.1    Moore, J.G.2    Chrispeels, M.J.3    Loris, R.4    Wyns, L.5
  • 17
    • 0035946982 scopus 로고    scopus 로고
    • Weak protein-protein interactions in lectins: The crystal structure of a vegetative lectin from the legume Dolichos biflorus
    • Buts L., Dao-Thi M.H., Loris R., Wyns L., Etzler M., Hamelryck T. Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus. J. Mol. Biol. 309:2001;193-201.
    • (2001) J. Mol. Biol. , vol.309 , pp. 193-201
    • Buts, L.1    Dao-Thi, M.H.2    Loris, R.3    Wyns, L.4    Etzler, M.5    Hamelryck, T.6
  • 18
    • 0031938173 scopus 로고    scopus 로고
    • Peptide mimotopes of carbohydrate antigens
    • Kieber-Emmons T. Peptide mimotopes of carbohydrate antigens. Immunol. Res. 17:1998;95-108.
    • (1998) Immunol. Res. , vol.17 , pp. 95-108
    • Kieber-Emmons, T.1
  • 19
    • 0033062668 scopus 로고    scopus 로고
    • Towards the development of peptide mimotopes of carbohydrate antigens as cancer vaccines
    • Qiu J., Luo P., Wasmund K., Steplewski Z., Kieber-Emmons T. Towards the development of peptide mimotopes of carbohydrate antigens as cancer vaccines. Hybridoma. 18:1999;103-112.
    • (1999) Hybridoma , vol.18 , pp. 103-112
    • Qiu, J.1    Luo, P.2    Wasmund, K.3    Steplewski, Z.4    Kieber-Emmons, T.5
  • 22
    • 0031058735 scopus 로고    scopus 로고
    • Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety
    • Kaur K.J., Khurana S., Salunke D.M. Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety. J. Biol. Chem. 272:1997;5539-5543.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5539-5543
    • Kaur, K.J.1    Khurana, S.2    Salunke, D.M.3
  • 24
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt G.J., Jones T.A. Phi/psi-chology: Ramachandran revisited. Structure. 4:1996;1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 26
    • 0023644678 scopus 로고
    • Refinement of crystal structure of wheat-germ agglutinin isolectin 2 at 1.8 Å resolution
    • Wright C.S. Refinement of crystal structure of wheat-germ agglutinin isolectin 2 at 1.8 Å resolution. J. Mol. Biol. 194:1987;501-529.
    • (1987) J. Mol. Biol. , vol.194 , pp. 501-529
    • Wright, C.S.1
  • 27
    • 0024962466 scopus 로고
    • Comparison of the refined crystal structures of two wheat-germ isolectins
    • Wright C.S. Comparison of the refined crystal structures of two wheat-germ isolectins. J. Mol. Biol. 209:1989;475-487.
    • (1989) J. Mol. Biol. , vol.209 , pp. 475-487
    • Wright, C.S.1
  • 28
    • 0034737303 scopus 로고    scopus 로고
    • Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose
    • Harata K., Muraki M. Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose. J. Mol. Biol. 297:2000;673-681.
    • (2000) J. Mol. Biol. , vol.297 , pp. 673-681
    • Harata, K.1    Muraki, M.2
  • 29
    • 0034660570 scopus 로고    scopus 로고
    • Crystal structure of Urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II
    • Saul F.A., Rovira P., Boulot G., Damme E.J., Peumans W.J., Truffa-Bachi P., Bentley G. Crystal structure of Urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II. Structure. 8:2000;593-603.
    • (2000) Structure. , vol.8 , pp. 593-603
    • Saul, F.A.1    Rovira, P.2    Boulot, G.3    Damme, E.J.4    Peumans, W.J.5    Truffa-Bachi, P.6    Bentley, G.7
  • 30
    • 0029013978 scopus 로고
    • The interaction of hevein with N-acetylglucosamine-containing oligosaccharides. Solution structure of hevein complexed to chitobiose
    • Asensio J.L., Canada F.J., Bruix M., Rodriguez-Romero A., Jimenez-Barbero J. The interaction of hevein with N-acetylglucosamine- containing oligosaccharides. Solution structure of hevein complexed to chitobiose. Eur. J. Biochem. 230:1995;1380-1382.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 1380-1382
    • Asensio, J.L.1    Canada, F.J.2    Bruix, M.3    Rodriguez-Romero, A.4    Jimenez-Barbero, J.5
  • 31
    • 0021755746 scopus 로고
    • Structural comparison of the two distinct sugar binding sites in wheat-germ agglutinin isolectin II
    • Wright C.S. Structural comparison of the two distinct sugar binding sites in wheat-germ agglutinin isolectin II. J. Mol. Biol. 178:1984;91-104.
    • (1984) J. Mol. Biol. , vol.178 , pp. 91-104
    • Wright, C.S.1
  • 32
    • 0026716436 scopus 로고
    • Crystal structure of a wheat-germ agglutinin/glycophorin- sialoglycopeptide receptor complex
    • Wright C.S. Crystal structure of a wheat-germ agglutinin/glycophorin- sialoglycopeptide receptor complex. J. Biol. Chem. 267:1992;14345-14352.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14345-14352
    • Wright, C.S.1
  • 33
    • 0025721792 scopus 로고
    • Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat-germ agglutinin
    • Wright H.T., Sandrasegaram G., Wright C.S. Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat-germ agglutinin. J. Mol. Evol. 33:1991;283-294.
    • (1991) J. Mol. Evol. , vol.33 , pp. 283-294
    • Wright, H.T.1    Sandrasegaram, G.2    Wright, C.S.3
  • 34
    • 34249919394 scopus 로고
    • Hevein: An antifungal protein from rubber-tree (Hevea brasiliensis) latex
    • Van Parijs J., Broekaert W.F., Goldstein I.J., Peumans W.J. Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta. 183:1991;258-264.
    • (1991) Planta , vol.183 , pp. 258-264
    • Van Parijs, J.1    Broekaert, W.F.2    Goldstein, I.J.3    Peumans, W.J.4
  • 35
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis W., Brown J.H., Cusack S., Paulson J.C., Skehel J.J., Wiley D.C. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature. 333:1988;426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 36
    • 0031252619 scopus 로고    scopus 로고
    • Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus agglutinin
    • Transue T.R., Smith A.K., Mo H., Goldstein I.J., Saper M.A. Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus agglutinin. Nature Struct. Biol. 26:1997;779-783.
    • (1997) Nature Struct. Biol. , vol.26 , pp. 779-783
    • Transue, T.R.1    Smith, A.K.2    Mo, H.3    Goldstein, I.J.4    Saper, M.A.5
  • 38
    • 0028987792 scopus 로고
    • Ligand-induced perturbations in Ultica dioica agglutinin
    • Hom K., Gochin M., Peumans W.J., Shine N. Ligand-induced perturbations in Ultica dioica agglutinin. FEBS Letters. 361:1995;157-161.
    • (1995) FEBS Letters , vol.361 , pp. 157-161
    • Hom, K.1    Gochin, M.2    Peumans, W.J.3    Shine, N.4
  • 39
    • 0031825894 scopus 로고    scopus 로고
    • Thermodynamic parameters of the interaction of Ultica dioica agglutinin with N-acetylglucosamine and its oligomers
    • Lee R.T., Gabius H.J., Lee Y.C. Thermodynamic parameters of the interaction of Ultica dioica agglutinin with N-acetylglucosamine and its oligomers. Glycoconjugate J. 15:1998;649-655.
    • (1998) Glycoconjugate J. , vol.15 , pp. 649-655
    • Lee, R.T.1    Gabius, H.J.2    Lee, Y.C.3
  • 40
    • 0034761895 scopus 로고    scopus 로고
    • Structure of Urtica dioica agglutinin isolectin I: Dimer formation mediated by two zinc ions bound at the sugar-binding site
    • Harata K., Schubert W.D., Muraki M. Structure of Urtica dioica agglutinin isolectin I: dimer formation mediated by two zinc ions bound at the sugar-binding site. Acta Crystallog. sect. D. 57:2001;1513-1517.
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1513-1517
    • Harata, K.1    Schubert, W.D.2    Muraki, M.3
  • 43
    • 0030720932 scopus 로고    scopus 로고
    • X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin
    • Olsen L.R., Dessen A., Guputa D., Sabesam S., Sacchettini J.C., Brewer C.F. X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin. Biochemistry. 36:1997;15073-15080.
    • (1997) Biochemistry , vol.36 , pp. 15073-15080
    • Olsen, L.R.1    Dessen, A.2    Guputa, D.3    Sabesam, S.4    Sacchettini, J.C.5    Brewer, C.F.6
  • 44
    • 0028359877 scopus 로고
    • Homogeneous aggregation of the 14-kDa β-galactoside specific vertebrate lectin complex with asialofetuin in mixed systems
    • Gupta D., Brewer C.F. Homogeneous aggregation of the 14-kDa β-galactoside specific vertebrate lectin complex with asialofetuin in mixed systems. Biochemistry. 33:1994;5526-5530.
    • (1994) Biochemistry , vol.33 , pp. 5526-5530
    • Gupta, D.1    Brewer, C.F.2
  • 45
    • 0028778145 scopus 로고
    • Observation of unique cross-linked lattices between multiantennary carbohydrates and soybean lectin. Presence of pseudo-2-fold axes of symmetry in complex type carbohydrates
    • Gupta D., Bhattacharyya L., Fant J., Macaluso F., Sabesan S., Brewer C.F. Observation of unique cross-linked lattices between multiantennary carbohydrates and soybean lectin. Presence of pseudo-2-fold axes of symmetry in complex type carbohydrates. Biochemistry. 33:1994;7495-7504.
    • (1994) Biochemistry , vol.33 , pp. 7495-7504
    • Gupta, D.1    Bhattacharyya, L.2    Fant, J.3    Macaluso, F.4    Sabesan, S.5    Brewer, C.F.6
  • 46
    • 0034717303 scopus 로고    scopus 로고
    • Structural and functional consequences of peptide-carbohydrate mimicry
    • Jain D., Kaur K.J., Sundaravadivel B., Salunke D.M. Structural and functional consequences of peptide-carbohydrate mimicry. J. Biol. Chem. 275:2000;16098-16102.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16098-16102
    • Jain, D.1    Kaur, K.J.2    Sundaravadivel, B.3    Salunke, D.M.4
  • 47
    • 0035014622 scopus 로고    scopus 로고
    • Plasticity in protein-peptide recognition: Crystal structures of two different peptides bound to concanavalin A
    • Jain D., Kaur K.J., Salunke D.M. Plasticity in protein-peptide recognition: crystal structures of two different peptides bound to concanavalin A. Biophys. J. 80:2001;2912-2921.
    • (2001) Biophys. J. , vol.80 , pp. 2912-2921
    • Jain, D.1    Kaur, K.J.2    Salunke, D.M.3
  • 48
    • 0035874139 scopus 로고    scopus 로고
    • Crystal structures of the peanut lectin-lactose complex at acidic pH: Retention of unusual quaternary structure, empty and carbohydrate bound combining site, molecular mimicry and crystal packing directed by interactions at the combining site
    • Ravishankar R., Thomas C.J., Suguna K., Surolia A., Vijayan M. Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining site, molecular mimicry and crystal packing directed by interactions at the combining site. Proteins: Struct. Funct. Genet. 43:2001;260-270.
    • (2001) Proteins: Struct. Funct. Genet. , vol.43 , pp. 260-270
    • Ravishankar, R.1    Thomas, C.J.2    Suguna, K.3    Surolia, A.4    Vijayan, M.5
  • 49
    • 0037778956 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of lectin C from the roots of pokeweed (Phytolacca americana)
    • Hayashida M., Fujii T., Hamasu M., Ishiguro M., Hata Y. Crystallization and preliminary X-ray analysis of lectin C from the roots of pokeweed (Phytolacca americana). Acta Crystallog. sect. D. 59:2003;1249-1252.
    • (2003) Acta Crystallog. sect. D , vol.59 , pp. 1249-1252
    • Hayashida, M.1    Fujii, T.2    Hamasu, M.3    Ishiguro, M.4    Hata, Y.5
  • 52
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 277:1997;307-326.
    • (1997) Methods Enzymol. , vol.277 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 53
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Warrington UK: SERC Daresbury Laboratory
    • Otwinowski Z. Maximum likelihood refinement of heavy atom parameters. Wolf W., Evans P.R., Leslie A.G.W. Isomorphous Replacement and Anomalous Scattering. 1991;80-86 SERC Daresbury Laboratory, Warrington UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 54
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 55
    • 0002583957 scopus 로고
    • DM: An automated procedure for phase improvement by density modification
    • Cowtan K. DM: an automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsletter Protein Crystallog. 31:1994;34-38.
    • (1994) Joint CCP4 ESF-EACBM Newsletter Protein Crystallog. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 56
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/XView
    • McRee D.E. A visual protein crystallographic software system for X11/XView. J. Mol. Graph. 10:1992;44-46.
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • Mcree, D.E.1
  • 58
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R.A. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1
  • 59
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30:1997;1022-1025.
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 60
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 61
    • 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. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 62
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.