메뉴 건너뛰기




Volumn 255, Issue 5, 1996, Pages 753-766

Molecular interaction between the strep-lag affinity peptide and its cognate target, streptavidin

Author keywords

Ligand affinity; Peptide spot assay; Protein engineering; Protein peptide complex; X ray crystallography

Indexed keywords

BIOTIN; HYBRID PROTEIN; PEPTIDE; RECOMBINANT PROTEIN; STREPTAVIDIN; SYNTHETIC PEPTIDE;

EID: 0029865819     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0061     Document Type: Article
Times cited : (283)

References (40)
  • 1
    • 0024519918 scopus 로고
    • Postsecretory modifications of streptavidin
    • Bayer, E. A., Ben-Hur, H., Hiller, Y. & Wilchek, M. (1989). Postsecretory modifications of streptavidin. Biochem. J. 259, 369-376.
    • (1989) Biochem. J. , vol.259 , pp. 369-376
    • Bayer, E.A.1    Ben-Hur, H.2    Hiller, Y.3    Wilchek, M.4
  • 2
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992a). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 335, 472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brünger, A.T.1
  • 3
    • 0003246845 scopus 로고
    • X-PLOR, Version 3.1
    • Yale University Press, New Haven, USA and London, UK
    • Brünger, A. T. (1992b). X-PLOR, Version 3.1, A System for X-ray Crystallography and NMR. Yale University Press, New Haven, USA and London, UK.
    • (1992) A System for X-ray Crystallography and NMR
    • Brünger, A.T.1
  • 4
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free r value. Methods and applications
    • Brünger, A. T. (1993). Assessment of phase accuracy by cross validation: the free r value. Methods and applications. Acta Crystallog. sect. D, 49, 24-36.
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 24-36
    • Brünger, A.T.1
  • 5
    • 0028011373 scopus 로고
    • Mass spectrometry - A useful tool for the protein X-ray crystallographer and NMR spectroscopist
    • Chait, B. T. (1994). Mass spectrometry - a useful tool for the protein X-ray crystallographer and NMR spectroscopist. Structure, 2, 465-467.
    • (1994) Structure , vol.2 , pp. 465-467
    • Chait, B.T.1
  • 6
    • 0025004285 scopus 로고
    • Random peptide libraries: A source of specific protein binding molecules
    • Devlin, J. J., Panganiban, L. C. & Devlin, P. E. (1990). Random peptide libraries: a source of specific protein binding molecules. Science, 249, 404-406.
    • (1990) Science , vol.249 , pp. 404-406
    • Devlin, J.J.1    Panganiban, L.C.2    Devlin, P.E.3
  • 7
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.1    Huber, R.2
  • 8
    • 0026656122 scopus 로고
    • Spot synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank, R. (1992). Spot synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron, 48, 9217-9232.
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 10
    • 77957001732 scopus 로고
    • Reaction of protein sulfhydryl groups with Ellman's reagent
    • Habeeb, A. F. S. A. (1972). Reaction of protein sulfhydryl groups with Ellman's reagent. Methods Enzymol. 37, 457-464.
    • (1972) Methods Enzymol. , vol.37 , pp. 457-464
    • Habeeb, A.F.S.A.1
  • 11
    • 0024653594 scopus 로고
    • Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchroton radiation
    • Hendrickson, W. A., Pähler, A., Smith, J. L., Satow, Y., Merritt, E. A. & Phizackerley R. P. (1989). Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchroton radiation. Proc. Natl Acad. Sci. USA, 86, 2190-2194.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2190-2194
    • Hendrickson, W.A.1    Pähler, A.2    Smith, J.L.3    Satow, Y.4    Merritt, E.A.5    Phizackerley, R.P.6
  • 12
    • 0000046837 scopus 로고
    • A highly potent analogue of oxytocin, desaminooxytocin
    • Hope, D. B., Murti, V. V. S. & Du Vigneaud, V. (1962). A highly potent analogue of oxytocin, desaminooxytocin. J. Biol. Chem. 237, 1563-1566.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1563-1566
    • Hope, D.B.1    Murti, V.V.S.2    Du Vigneaud, V.3
  • 13
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of error in these models
    • Jones, A., Zou, J.-Y., Cowan, S. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of error in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 14
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 15
    • 0028798287 scopus 로고
    • Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes
    • Kleymann, G., Ostermeier, C., Ludwig, B., Skerra, A. & Michel, H. (1995). Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes. BioTechnology, 13, 155-160.
    • (1995) Biotechnology , vol.13 , pp. 155-160
    • Kleymann, G.1    Ostermeier, C.2    Ludwig, B.3    Skerra, A.4    Michel, H.5
  • 16
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • Lam, K. S., Salmon, S. E., Hersh, E. M., Hruby V. J., Kazmierski, W. M. & Knapp, R. J. (1991). A new type of synthetic peptide library for identifying ligand-binding activity Nature, 354, 82-84.
    • (1991) Nature , vol.354 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 17
    • 0027164314 scopus 로고
    • Three-dimensional structures of avidin and the avidin-biotin complex
    • Livnah, O., Bayer, E. A., Wilchek, M. & Sussman, J. L. (1993). Three-dimensional structures of avidin and the avidin-biotin complex. Proc. Natl Acad. Sci. USA, 90, 5076-5080.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5076-5080
    • Livnah, O.1    Bayer, E.A.2    Wilchek, M.3    Sussman, J.L.4
  • 18
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzzati, V. (1952). Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. sect. A, 5, 802-810.
    • (1952) Acta Crystallog. Sect. A , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 19
    • 0000548829 scopus 로고
    • Three-dimensional structure of peptide-protein complexes: Implications for recognition
    • Marshall, G. R. (1992). Three-dimensional structure of peptide-protein complexes: implications for recognition. Curr. Opin. Struct. Biol. 2, 904-919.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 904-919
    • Marshall, G.R.1
  • 20
    • 0027253452 scopus 로고
    • M13 bacteriophage displaying disulfide-constrained microproteins
    • McLafferty M. A., Kent, R. B., Ladner, R. C. & Markland, W. (1993). M13 bacteriophage displaying disulfide-constrained microproteins. Gene, 128, 29-36.
    • (1993) Gene , vol.128 , pp. 29-36
    • McLafferty, M.A.1    Kent, R.B.2    Ladner, R.C.3    Markland, W.4
  • 21
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield, B. (1986). Solid phase synthesis. Science, 232, 341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, B.1
  • 22
    • 0028138405 scopus 로고
    • Grafting of a high-affinity Zn(II)-binding site on the β-barrel of retinol-binding protein results in enhanced folding stability and enables simplified purification
    • Müller, H. N. & Skerra, A. (1994). Grafting of a high-affinity Zn(II)-binding site on the β-barrel of retinol-binding protein results in enhanced folding stability and enables simplified purification. Biochemistry, 33, 14126-14135.
    • (1994) Biochemistry , vol.33 , pp. 14126-14135
    • Müller, H.N.1    Skerra, A.2
  • 23
    • 0028287188 scopus 로고
    • Engineering proteins to facilitate bioprocessing
    • Nygren, P.-Å., Ståhl, S. & Uhlén, M. (1994). Engineering proteins to facilitate bioprocessing. Trends Biotechnol. 12, 184-188.
    • (1994) Trends Biotechnol. , vol.12 , pp. 184-188
    • Nygren, P.-A.1    Ståhl, S.2    Uhlén, M.3
  • 25
    • 0028872393 scopus 로고
    • Crystals of an antibody Fv fragment against an integral membrane protein diffracting to 1.28 Å resolution
    • Ostermeier, C., Essen, L.-O. & Michel, H. (1995). Crystals of an antibody Fv fragment against an integral membrane protein diffracting to 1.28 Å resolution. Proteins: Struct. Funct. Genet. 21, 74-77.
    • (1995) Proteins: Struct. Funct. Genet. , vol.21 , pp. 74-77
    • Ostermeier, C.1    Essen, L.-O.2    Michel, H.3
  • 27
    • 0027214259 scopus 로고
    • Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 Å resolution
    • Pugliese, L., Coda, A., Malcovati, M. & Bolognesi, M. (1993). Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 Å resolution. J. Mol. Biol. 231, 698-710.
    • (1993) J. Mol. Biol. , vol.231 , pp. 698-710
    • Pugliese, L.1    Coda, A.2    Malcovati, M.3    Bolognesi, M.4
  • 29
    • 0027247924 scopus 로고
    • Biotin binders selected from a random peptide library expressed on phage
    • Saggio, I. & Laufer, R. (1993). Biotin binders selected from a random peptide library expressed on phage. Biochem. J. 293, 613-616.
    • (1993) Biochem. J. , vol.293 , pp. 613-616
    • Saggio, I.1    Laufer, R.2
  • 30
    • 0027499708 scopus 로고
    • The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment
    • Schmidt, T. G. M. & Skerra, A. (1993). The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment. Protein Eng. 6, 109-122.
    • (1993) Protein Eng. , vol.6 , pp. 109-122
    • Schmidt, T.G.M.1    Skerra, A.2
  • 31
    • 0027991404 scopus 로고
    • One-step affinity purification of bacterially produced proteins by means of the "Strep tag" and immobilized recombinant core streptavidin
    • Schmidt, T. G. M. & Skerra, A. (1994a). One-step affinity purification of bacterially produced proteins by means of the "Strep tag" and immobilized recombinant core streptavidin. J. Chromatog. sect. A, 676, 337-345.
    • (1994) J. Chromatog. Sect. A , vol.676 , pp. 337-345
    • Schmidt, T.G.M.1    Skerra, A.2
  • 32
    • 0028044571 scopus 로고
    • The bilin-binding protein of Pieris brassicae - cDNA sequence and regulation of expression reveal distinct features of this insect pigment protein
    • Schmidt, F. S. & Skerra, A. (1994b). The bilin-binding protein of Pieris brassicae - cDNA sequence and regulation of expression reveal distinct features of this insect pigment protein. Eur. J. Biochem. 219, 855-863.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 855-863
    • Schmidt, F.S.1    Skerra, A.2
  • 33
    • 0016160429 scopus 로고
    • Measurement of protein by spectrophotometry at 205 nm
    • Scopes, R. K. (1974). Measurement of protein by spectrophotometry at 205 nm. Anal. Biochem. 59, 277-282.
    • (1974) Anal. Biochem. , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 34
    • 0026654781 scopus 로고
    • Discovering peptide ligands using epitope libraries
    • Scott, J. K. (1992). Discovering peptide ligands using epitope libraries. Trends Biochem. Sci. 17, 241-245.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 241-245
    • Scott, J.K.1
  • 35
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber, P. C., Ohlendorf, D. H., Wendoloski, J. J. & Salemme, F. R. (1989). Structural origins of high-affinity biotin binding to streptavidin. Science, 243, 85-88.
    • (1989) Science , vol.243 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4
  • 36
    • 0026807019 scopus 로고
    • Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin
    • Weber, P. C., Pantoliano, M. W. & Thompson, L. D. (1992a). Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin. Biochemistry, 31, 9350-9354.
    • (1992) Biochemistry , vol.31 , pp. 9350-9354
    • Weber, P.C.1    Pantoliano, M.W.2    Thompson, L.D.3
  • 37
    • 0026606240 scopus 로고
    • Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin
    • Weber, P. C., Wendoloski, J. J., Pantoliano, M. W. & Salemme, F. R. (1992b). Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin. J. Am. Chem. Soc. 114, 3197-3200.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3197-3200
    • Weber, P.C.1    Wendoloski, J.J.2    Pantoliano, M.W.3    Salemme, F.R.4
  • 38
    • 0024741801 scopus 로고
    • Avidin-biotin technology ten years on: Has it lived up to its expectations?
    • Wilchek, M. & Bayer, E. A. (1989). Avidin-biotin technology ten years on: has it lived up to its expectations? Trends Biochem. Sci. 14, 408-412.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 408-412
    • Wilchek, M.1    Bayer, E.A.2
  • 39
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J. F. & Lin, L.-N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 40
    • 0028861262 scopus 로고
    • Binding epitope of somatostatin defined by phage-displayed peptide libraries
    • Wright, R. M., Gram, H., Vattay A., Byrne, S., Lake, P. & Dottavio, D. (1995). Binding epitope of somatostatin defined by phage-displayed peptide libraries. BioTechnology, 13, 165-169.
    • (1995) Biotechnology , vol.13 , pp. 165-169
    • Wright, R.M.1    Gram, H.2    Vattay, A.3    Byrne, S.4    Lake, P.5    Dottavio, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.