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Volumn 61, Issue 17, 2004, Pages 2184-2188

Lanthanide-binding peptides and the enzymes that Might Have Been

Author keywords

De novo design; Lanthanides; Rare earths

Indexed keywords

CALCIUM DERIVATIVE; CALCIUM ION; ENDONUCLEASE; LANTHANIDE; LEWIS ACID; NUCLEASE; PEPTIDE DERIVATIVE;

EID: 4644281704     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-4156-2     Document Type: Review
Times cited : (71)

References (33)
  • 1
    • 4644351405 scopus 로고    scopus 로고
    • note
    • Lanthanides are ideal calcium analogs due to the chemical similarities of the ions, including ionic radii, coordination environments and ligand preferences. The ionic radius of Ca(II) ion is 0.99 Å, and the ionic radii of lanthanides range from 0.86 to 1.22 Å. Coordination numbers of calcium ion vary from 6 to 8, and those of lanthanide ions typically range from 8 to 9. In addition, both calcium and lanthanide ions have a strong preference for hard oxygen donor ligands, and can adopt flexible geometries mainly governed by steric factors. As such, the lanthanide ions can substitute for calcium in proteins with minimal structural changes.
  • 3
    • 0025355493 scopus 로고
    • Calcium(II) site specificity: Effect of size and charge on metal ion binding to and EF-hand-like site
    • Snyder E. E., Buoscio B. W. and Falke J. J. (1990) Calcium(II) site specificity: effect of size and charge on metal ion binding to and EF-hand-like site. Biochemistry 29: 3937-3943
    • (1990) Biochemistry , vol.29 , pp. 3937-3943
    • Snyder, E.E.1    Buoscio, B.W.2    Falke, J.J.3
  • 4
    • 0036592083 scopus 로고    scopus 로고
    • Lanthanide complexes in molecular recognition and chirality sensing of biological substrates
    • Tsukube H. and Shinoda S. (2002) Lanthanide complexes in molecular recognition and chirality sensing of biological substrates. Chem. Rev. 102: 2389-2403
    • (2002) Chem. Rev. , vol.102 , pp. 2389-2403
    • Tsukube, H.1    Shinoda, S.2
  • 5
    • 0033363494 scopus 로고    scopus 로고
    • Gadolinium(III) chelates as MRI contrast agents: Structure, dynamics and applications
    • Caravan P., Ellison J. J., McMurry T. J. and Lauffer R. B. (1999) Gadolinium(III) chelates as MRI contrast agents: structure, dynamics and applications. Chem. Rev. 99: 2292-2352
    • (1999) Chem. Rev. , vol.99 , pp. 2292-2352
    • Caravan, P.1    Ellison, J.J.2    McMurry, T.J.3    Lauffer, R.B.4
  • 6
    • 0036625261 scopus 로고    scopus 로고
    • Chiral lanthanide complexes: Coordination chemistry and applications
    • Aspinall H. C. (2002) Chiral lanthanide complexes: coordination chemistry and applications. Chem. Rev. 102: 1807-1850
    • (2002) Chem. Rev. , vol.102 , pp. 1807-1850
    • Aspinall, H.C.1
  • 7
    • 0024498387 scopus 로고
    • Conformation and ion binding properties of peptides related to calcium binding domain III of bovine brain calmodulin
    • Borin G., Ruzza P., Rossi M., Calderan A., Marchiori F. and Peggion E. (1989) Conformation and ion binding properties of peptides related to calcium binding domain III of bovine brain calmodulin. Biopolymers 28: 353-369
    • (1989) Biopolymers , vol.28 , pp. 353-369
    • Borin, G.1    Ruzza, P.2    Rossi, M.3    Calderan, A.4    Marchiori, F.5    Peggion, E.6
  • 8
    • 0021101593 scopus 로고
    • Lanthanide-induced peptide folding: Variations in lanthanide affinity and induced peptide conformation
    • Gariépy J., Sykes B. D. and Hodges R. S. (1983) Lanthanide-induced peptide folding: variations in lanthanide affinity and induced peptide conformation. Biochemistry 22: 1765-1772
    • (1983) Biochemistry , vol.22 , pp. 1765-1772
    • Gariépy, J.1    Sykes, B.D.2    Hodges, R.S.3
  • 9
    • 0037103427 scopus 로고    scopus 로고
    • Steady-state luminescence investigation of the binding of Eu(III) and Tb(III) ions with synthetic peptides derived from plant thionins
    • Bemquerer M. P., Bloch C., Brito H. F., Teotonio E. E. S. and Miranda M. T. M. (2002) Steady-state luminescence investigation of the binding of Eu(III) and Tb(III) ions with synthetic peptides derived from plant thionins. J. Inorg. Biochem. 91: 363-370
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 363-370
    • Bemquerer, M.P.1    Bloch, C.2    Brito, H.F.3    Teotonio, E.E.S.4    Miranda, M.T.M.5
  • 11
    • 0039740776 scopus 로고    scopus 로고
    • Isolated calcium-binding loops of EF-hand proteins can dimerize to form a native-like structure
    • Wójcik J., Góral J., Pawlowski K. and Bierzynski A. (1997) Isolated calcium-binding loops of EF-hand proteins can dimerize to form a native-like structure. Biochemistry 36: 680-687
    • (1997) Biochemistry , vol.36 , pp. 680-687
    • Wójcik, J.1    Góral, J.2    Pawlowski, K.3    Bierzynski, A.4
  • 13
    • 0030993346 scopus 로고    scopus 로고
    • Calcium binding peptides from α-lactalbumin: Implications for protein folding and stability
    • Kuhlman B., Boice J. A., Wu W. J., Fairman R. and Raleigh D. P. (1997) Calcium binding peptides from α-lactalbumin: implications for protein folding and stability. Biochemistry 36: 4607-4615
    • (1997) Biochemistry , vol.36 , pp. 4607-4615
    • Kuhlman, B.1    Boice, J.A.2    Wu, W.J.3    Fairman, R.4    Raleigh, D.P.5
  • 14
    • 0032542575 scopus 로고    scopus 로고
    • Metal ion induced folding of a de novo designed coiled-coil peptide
    • Kohn W. D., Kay C. M., Sykes B. D. and Hodges R. S. (1998) Metal ion induced folding of a de novo designed coiled-coil peptide. J. Am. Chem. Soc. 120: 1124-1132
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1124-1132
    • Kohn, W.D.1    Kay, C.M.2    Sykes, B.D.3    Hodges, R.S.4
  • 15
    • 0037133590 scopus 로고    scopus 로고
    • Engineering a terbium-binding site into an integral membrane protein for luminescence energy transfer
    • Vázquez-Ibar J. L., Weinglass A. B. and Kaback H. R. (2002) Engineering a terbium-binding site into an integral membrane protein for luminescence energy transfer. Proc. Natl. Acad. Sci. USA 99: 3487-3492
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3487-3492
    • Vázquez-Ibar, J.L.1    Weinglass, A.B.2    Kaback, H.R.3
  • 16
    • 0037419262 scopus 로고    scopus 로고
    • A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides
    • Nitz M., Franz K. J., Maglathlin R. L. and Imperiali B. (2003) A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides. ChemBioChem 4: 272-276
    • (2003) ChemBioChem , vol.4 , pp. 272-276
    • Nitz, M.1    Franz, K.J.2    Maglathlin, R.L.3    Imperiali, B.4
  • 17
    • 0026655017 scopus 로고
    • Comparison of terbium(III) luminscence enhancement in mutants of EF hand calcium binding proteins
    • Hogue C. W. V., MacManus J. P., Banville D. and Szabo A. G. (1992) Comparison of terbium(III) luminscence enhancement in mutants of EF hand calcium binding proteins. J. Biol. Chem. 267: 13340-13347
    • (1992) J. Biol. Chem. , vol.267 , pp. 13340-13347
    • Hogue, C.W.V.1    MacManus, J.P.2    Banville, D.3    Szabo, A.G.4
  • 18
    • 0037419375 scopus 로고    scopus 로고
    • Lanthanide-binding tags as versatile protein coexpression probes
    • Franz K. J., Nitz M. and Imperiali B. (2003) Lanthanide-binding tags as versatile protein coexpression probes. ChemBioChem 4: 265-271
    • (2003) ChemBioChem , vol.4 , pp. 265-271
    • Franz, K.J.1    Nitz, M.2    Imperiali, B.3
  • 19
    • 0242299265 scopus 로고    scopus 로고
    • Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings
    • Wöhnert J., Franz K. J., Nitz M., Imperiali B. and Schwalbe H. (2003) Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings. J. Am. Chem. Soc. 125: 13338-13339
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13338-13339
    • Wöhnert, J.1    Franz, K.J.2    Nitz, M.3    Imperiali, B.4    Schwalbe, H.5
  • 20
    • 0142094035 scopus 로고    scopus 로고
    • Gadolinium-binding helix-turn-helix peptides: DNA-dependent MRI contrast agents
    • Caravan P., Greenwood J. M., Welch J. T. and Franklin S. J. (2003) Gadolinium-binding helix-turn-helix peptides: DNA-dependent MRI contrast agents. Chem. Commun. 20: 2574-2575
    • (2003) Chem. Commun. , vol.20 , pp. 2574-2575
    • Caravan, P.1    Greenwood, J.M.2    Welch, J.T.3    Franklin, S.J.4
  • 21
    • 0035313441 scopus 로고    scopus 로고
    • Lanthanide mediated DNA hydrolysis
    • Franklin S. J. (2001) Lanthanide mediated DNA hydrolysis. Curr. Opin. Chem. Biol. 5: 201-208
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 201-208
    • Franklin, S.J.1
  • 22
    • 0033592217 scopus 로고    scopus 로고
    • Hydrolysis of DNA and RNA by lanthanide ions: Mechanistic studies leading to new applications
    • Komiyama M. (1999) Hydrolysis of DNA and RNA by lanthanide ions: mechanistic studies leading to new applications. Chem. Commun. 16: 1443-1451
    • (1999) Chem. Commun. , vol.16 , pp. 1443-1451
    • Komiyama, M.1
  • 23
    • 0032090901 scopus 로고    scopus 로고
    • Toward the development of metal-based synthetic nucleases and peptidases: A rationale and progress report in applying the principles of coordination chemistry
    • Hegg E. L. and Burstyn J. N. (1998) Toward the development of metal-based synthetic nucleases and peptidases: a rationale and progress report in applying the principles of coordination chemistry. Coord. Chem. Rev. 173: 133-165
    • (1998) Coord. Chem. Rev. , vol.173 , pp. 133-165
    • Hegg, E.L.1    Burstyn, J.N.2
  • 25
    • 0034257929 scopus 로고    scopus 로고
    • 2+-bound calmodulin: An analysis of disorder and implications for functionally relevant plasticity
    • 2+-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity. J. Mol. Biol. 301: 1237-1256
    • (2000) J. Mol. Biol. , vol.301 , pp. 1237-1256
    • Wilson, M.A.1    Brunger, A.T.2
  • 26
    • 0032573434 scopus 로고    scopus 로고
    • Engrailed homeodomain-DNA complex at 2.2 Å resolution: A detailed view of the interface and comparison with other engrailed structures
    • Fraenkel E., Rould M. A., Chambers K. A. and Pabo C. O. (1998) Engrailed homeodomain-DNA complex at 2.2 Å resolution: a detailed view of the interface and comparison with other engrailed structures. J. Mol. Biol. 284: 351-361
    • (1998) J. Mol. Biol. , vol.284 , pp. 351-361
    • Fraenkel, E.1    Rould, M.A.2    Chambers, K.A.3    Pabo, C.O.4
  • 27
    • 0037173575 scopus 로고    scopus 로고
    • Hydrolytically active Eu(III) and Ce(IV) EF-hand peptides
    • Sirish M. and Franklin S. J. (2002) Hydrolytically active Eu(III) and Ce(IV) EF-hand peptides. J. Inorg. Biochem. 91: 253-258
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 253-258
    • Sirish, M.1    Franklin, S.J.2
  • 28
    • 0037386541 scopus 로고    scopus 로고
    • Lanthanide-binding HTH peptides: Solution structure of a designed metallonuclease
    • Welch J. T., Kearney W. R. and Franklin S. J. (2003) Lanthanide-binding HTH peptides: solution structure of a designed metallonuclease. Proc. Natl. Acad. Sci. USA 100: 3725-3730
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3725-3730
    • Welch, J.T.1    Kearney, W.R.2    Franklin, S.J.3
  • 29
    • 0344586211 scopus 로고    scopus 로고
    • Europium luminescence of EF-hand HTH chimeras: Impact of pH and DNA-binding on europium coordination
    • Jain S., Welch J. T., Horrocks W. De W. Jr and Franklin S. J. (2003) Europium luminescence of EF-hand HTH chimeras: impact of pH and DNA-binding on europium coordination. Inorg. Chem. 42: 8098-8104
    • (2003) Inorg. Chem. , vol.42 , pp. 8098-8104
    • Jain, S.1    Welch, J.T.2    Horrocks Jr., W.D.W.3    Franklin, S.J.4
  • 31
    • 0037058862 scopus 로고    scopus 로고
    • pH dependent phosphate hydrolysis by a lanthanide EF-hand peptide
    • Kim Y. and Franklin S. J. (2002) pH dependent phosphate hydrolysis by a lanthanide EF-hand peptide. Inorg. Chim. Acta 341: 107-112
    • (2002) Inorg. Chim. Acta , vol.341 , pp. 107-112
    • Kim, Y.1    Franklin, S.J.2
  • 32
    • 0038657551 scopus 로고    scopus 로고
    • Sequence preference in DNA cleavage by a chimeric metallopeptide
    • Kovacic R. T., Welch J. T. and Franklin S. J. (2003) Sequence preference in DNA cleavage by a chimeric metallopeptide. J. Am. Chem. Soc. 125: 6656-6662
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6656-6662
    • Kovacic, R.T.1    Welch, J.T.2    Franklin, S.J.3
  • 33
    • 0028108227 scopus 로고
    • Differential DNA-binding specificity of the engrailed homeodomain: The role of residue 50
    • Ades S. E. and Sauer R. T. (1994) Differential DNA-binding specificity of the engrailed homeodomain: the role of residue 50. Biochemistry 33: 9187-9194
    • (1994) Biochemistry , vol.33 , pp. 9187-9194
    • Ades, S.E.1    Sauer, R.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.