메뉴 건너뛰기




Volumn 26, Issue , 1997, Pages 357-371

Lessons from zinc-binding peptides

Author keywords

Metal binding; Protein folding; Zinc finger

Indexed keywords

BINDING PROTEIN; METAL; NUCLEIC ACID; REGULATOR PROTEIN; ZINC FINGER PROTEIN;

EID: 0030983214     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.26.1.357     Document Type: Review
Times cited : (240)

References (48)
  • 2
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 angstroms resolution
    • Babu YS, Bugg CE, Cook WJ. 1988. Structure of calmodulin refined at 2.2 angstroms resolution. J. Mol. Biol. 204:191-204
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 3
    • 0029100766 scopus 로고
    • Depletion and replacement of protein metal ligands
    • Barrick D. 1995. Depletion and replacement of protein metal ligands. Curr. Opin. Biotechnol. 6:411-18
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 411-418
    • Barrick, D.1
  • 4
    • 0000957925 scopus 로고
    • On the metal ion specificity of "zinc finger" proteins
    • Berg JM, Merkle DL. 1989. On the metal ion specificity of "zinc finger" proteins. J. Am. Chem. Soc. 111:3759-61
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3759-3761
    • Berg, J.M.1    Merkle, D.L.2
  • 5
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg JM, Shi Y. 1996. The galvanization of biology: A growing appreciation for the roles of zinc. Science 271:1081-85
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 6
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou P, Fasman GD. 1973. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 13:211-22
    • (1973) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.1    Fasman, G.D.2
  • 7
    • 0028670569 scopus 로고
    • In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence
    • Choo Y, Sanchez-Garcia I, Klug A. 1994. In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence. Nature 372:642-45
    • (1994) Nature , vol.372 , pp. 642-645
    • Choo, Y.1    Sanchez-Garcia, I.2    Klug, A.3
  • 8
    • 0026766977 scopus 로고
    • Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins
    • Coleman JE. 1992. Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. Annu. Rev. Biochem. 61:897-946
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 897-946
    • Coleman, J.E.1
  • 9
    • 0027401045 scopus 로고
    • Use of a zinc-finger consensus sequence framework and specificity rules to design specific DNA binding proteins
    • Desjarlais JR, Berg JM. 1993. Use of a zinc-finger consensus sequence framework and specificity rules to design specific DNA binding proteins. Proc. Natl. Acad. Sci. USA 90:2256-60
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2256-2260
    • Desjarlais, J.R.1    Berg, J.M.2
  • 10
    • 0026766750 scopus 로고
    • Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasterianum rubredoxin
    • Eidsness MK, O'Dell SE, Kurtz DM Jr, Robson RL, Scott RA. 1992. Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasterianum rubredoxin. Protein Eng. 5:367-71
    • (1992) Protein Eng. , vol.5 , pp. 367-371
    • Eidsness, M.K.1    O'Dell, S.E.2    Kurtz Jr., D.M.3    Robson, R.L.4    Scott, R.A.5
  • 11
    • 0027170979 scopus 로고
    • Time-resolved energy transfer measurements of donor-acceptor distance distributions and intramolecular flexibility of a CCHH zinc-finger peptide
    • Eis PS, Lakowicz JR. 1993. Time-resolved energy transfer measurements of donor-acceptor distance distributions and intramolecular flexibility of a CCHH zinc-finger peptide. Biochemistry 32:7981-93
    • (1993) Biochemistry , vol.32 , pp. 7981-7993
    • Eis, P.S.1    Lakowicz, J.R.2
  • 12
    • 0023375317 scopus 로고
    • Metal-dependent folding of a single zinc finger from transcription factor IIIA
    • Frankel AD, Berg, JM, Pabo CO. 1987. Metal-dependent folding of a single zinc finger from transcription factor IIIA. Proc. Natl. Acad. Sci. USA 84:4841-45
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4841-4845
    • Frankel, A.D.1    Berg, J.M.2    Pabo, C.O.3
  • 13
    • 0029975181 scopus 로고    scopus 로고
    • A fluorescent zinc probe based on metal-induced peptide folding
    • Godwin HA, Berg JM. 1996. A fluorescent zinc probe based on metal-induced peptide folding. J. Am. Chem. Soc. 118:6514-15
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6514-6515
    • Godwin, H.A.1    Berg, J.M.2
  • 15
    • 0025995844 scopus 로고
    • A structural taxonomy of DNA-binding domains
    • Harrison SC. 1991. A structural taxonomy of DNA-binding domains. Nature 353:715-19
    • (1991) Nature , vol.353 , pp. 715-719
    • Harrison, S.C.1
  • 17
    • 0026466149 scopus 로고
    • Determination of the base recognition positions of zinc fingers from sequence analysis
    • Jacobs GH. 1992. Determination of the base recognition positions of zinc fingers from sequence analysis. EMBO. J. 11:4507-17
    • (1992) EMBO. J. , vol.11 , pp. 4507-4517
    • Jacobs, G.H.1
  • 19
    • 0027400789 scopus 로고
    • Aromatic-histidine interactions in the zinc finger motif: Structural inequivalence of phenylalanine and tyrosine in the hydrophobic core
    • Jasanoff A, Weiss MA. 1993. Aromatic-histidine interactions in the zinc finger motif: structural inequivalence of phenylalanine and tyrosine in the hydrophobic core. Biochemistry 32:1423-32
    • (1993) Biochemistry , vol.32 , pp. 1423-1432
    • Jasanoff, A.1    Weiss, M.A.2
  • 21
    • 0027411181 scopus 로고
    • Thermodynamic {β}-sheet propensities measured using a zinc-finger host peptide
    • Kim CA, Berg JM. 1993. Thermodynamic {β}-sheet propensities measured using a zinc-finger host peptide. Nature 362:267-70
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 24
    • 0027767784 scopus 로고
    • Co-chairman's remarks: Protein designs for the specific recognition of DNA
    • Klug A. 1993. Co-chairman's remarks: protein designs for the specific recognition of DNA. Gene 135:83-92
    • (1993) Gene , vol.135 , pp. 83-92
    • Klug, A.1
  • 25
    • 0029032723 scopus 로고
    • Protein motifs. 5. Zinc fingers
    • Klug A, Schwabe JW. 1995. Protein motifs. 5. Zinc fingers. FASEB J. 9:597-604
    • (1995) FASEB J. , vol.9 , pp. 597-604
    • Klug, A.1    Schwabe, J.W.2
  • 26
    • 0000933784 scopus 로고
    • A consensus zinc finger peptide: Design, high-affinity metal binding, a pH-dependent structure, and a His to Cys sequence variant
    • Krizek BA, Amann BT, Kilfoil VJ, Merkle DL, Berg JM. 1991. A consensus zinc finger peptide: design, high-affinity metal binding, a pH-dependent structure, and a His to Cys sequence variant. J. Am. Chem. Soc. 113:4518-23
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4518-4523
    • Krizek, B.A.1    Amann, B.T.2    Kilfoil, V.J.3    Merkle, D.L.4    Berg, J.M.5
  • 28
    • 0001505616 scopus 로고
    • Ligand variation and metal ion binding specificity in zinc finger peptides
    • Krizek BA, Merkle DL, Berg JM. 1993. Ligand variation and metal ion binding specificity in zinc finger peptides. Inorg. Chem. 32:937-40
    • (1993) Inorg. Chem. , vol.32 , pp. 937-940
    • Krizek, B.A.1    Merkle, D.L.2    Berg, J.M.3
  • 30
    • 0025260032 scopus 로고
    • Side-chain contributions to the stability of alpha-helical structure in peptides
    • Lyu PC, Liff MI, Marky LA, Kallenbach NR. 1990. Side-chain contributions to the stability of alpha-helical structure in peptides. Science 250:669-73
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 31
    • 84990437815 scopus 로고
    • Design and characterization of a ligand-binding metallopeptide
    • Merkle DL, Schmidt MH, Berg JM. 1991. Design and characterization of a ligand-binding metallopeptide. J. Am. Chem. Soc. 113:5450-51
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5450-5451
    • Merkle, D.L.1    Schmidt, M.H.2    Berg, J.M.3
  • 33
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller J, McLachlan AD, Klug A. 1985. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J. 4:1609-14
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 34
    • 8244258487 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 36
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • O'Haloran TV. 1993. Transition metals in control of gene expression. Science 261:715-25
    • (1993) Science , vol.261 , pp. 715-725
    • O'Haloran, T.V.1
  • 37
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil KT, DeGrado WF. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250:646-51
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 39
    • 0024290112 scopus 로고
    • Zinc-dependent structure of a single-finger domain of yeast ADR1
    • Parraga G, Horvath S, Eisen A, Taylor WE, Hood, et al. 1988. Zinc-dependent structure of a single-finger domain of yeast ADR1. Science 241:1489-92
    • (1988) Science , vol.241 , pp. 1489-1492
    • Parraga, G.1    Horvath, S.2    Eisen, A.3    Taylor, W.E.4    Hood5
  • 40
    • 0026808752 scopus 로고
    • Two-dimensional NMR studies of the zinc finger motif: Solution structures and dynamics of mutant ZFY domains containing aromatic substitutions in the hydrophobic core
    • Qian X, Wiess MA. 1992. Two-dimensional NMR studies of the zinc finger motif: solution structures and dynamics of mutant ZFY domains containing aromatic substitutions in the hydrophobic core. Biochemistry 31:7463-76
    • (1992) Biochemistry , vol.31 , pp. 7463-7476
    • Qian, X.1    Wiess, M.A.2
  • 41
    • 0027289198 scopus 로고
    • The design of metal-binding sites in proteins
    • Regan L. 1993. The design of metal-binding sites in proteins. Annu. Rev. Biophys. Biomol. Struct. 22:257-81
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 257-281
    • Regan, L.1
  • 42
    • 0029016430 scopus 로고
    • Protein design: Novel metal-binding sites
    • Regan L. 1995. Protein design: novel metal-binding sites. Trends Biochem. Sci. 20:280-85
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 280-285
    • Regan, L.1
  • 43
    • 0025644594 scopus 로고
    • A tetrahedral Zinc(II)-binding site introduced into a designed protein
    • Regan L, Clarke ND. 1990. A tetrahedral Zinc(II)-binding site introduced into a designed protein. Biochemistry 29:10878-83
    • (1990) Biochemistry , vol.29 , pp. 10878-10883
    • Regan, L.1    Clarke, N.D.2
  • 44
  • 45
    • 0028792105 scopus 로고
    • Guidelines for protein design: The energetics of {β}-sheet side-chain interactions
    • Smith CK, Regan L. 1995. Guidelines for protein design: The energetics of {β}-sheet side-chain interactions. Science 270:980-82
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 46
    • 0028175780 scopus 로고
    • A thermodynamic scale for the {β}-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L. 1994. A thermodynamic scale for the {β}-sheet forming tendencies of the amino acids. Biochemistry 33:5510-17
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 47
    • 0024540294 scopus 로고
    • Fluorescent indicators of ion concentrations
    • Tsien RY. 1989. Fluorescent indicators of ion concentrations. Methods Cell Biol. 30:127-56
    • (1989) Methods Cell Biol. , vol.30 , pp. 127-156
    • Tsien, R.Y.1
  • 48
    • 0001013690 scopus 로고    scopus 로고
    • Design and evaluation of a peptidyl fluorescent chemosensor for divalent zinc
    • Walkup GK, Imperiali B. 1996. Design and evaluation of a peptidyl fluorescent chemosensor for divalent zinc. J. Am. Chem. Soc. 118:3053-54
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3053-3054
    • Walkup, G.K.1    Imperiali, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.