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Volumn 363, Issue 2, 2006, Pages 460-468

Early Protein Evolution: Building Domains from Ligand-binding Polypeptide Segments

Author keywords

antibody; epitope vaccine; heme; lysozyme; protein folding

Indexed keywords

DIMER; F10 MONOCLONAL ANTIBODY; HEME; HYHEL 5 MONOCLONAL ANTIBODY; LYSOZYME; MONOCLONAL ANTIBODY; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 33748939410     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.031     Document Type: Article
Times cited : (35)

References (38)
  • 1
    • 0001126390 scopus 로고
    • Do genes-in-pieces imply proteins-in-pieces?
    • Blake C.C.F. Do genes-in-pieces imply proteins-in-pieces?. Nature 273 (1978) 267
    • (1978) Nature , vol.273 , pp. 267
    • Blake, C.C.F.1
  • 2
    • 0018263844 scopus 로고
    • Why genes in pieces?
    • Gilbert W. Why genes in pieces?. Nature 271 (1978) 501
    • (1978) Nature , vol.271 , pp. 501
    • Gilbert, W.1
  • 3
    • 0033052969 scopus 로고    scopus 로고
    • A hierarchical approach to protein molecular evolution
    • Bogarad L.D., and Deem M.W. A hierarchical approach to protein molecular evolution. Proc. Natl Acad. Sci. USA 96 (1999) 2591-2595
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2591-2595
    • Bogarad, L.D.1    Deem, M.W.2
  • 4
    • 0034730144 scopus 로고    scopus 로고
    • Novel folded protein domains generated by combinatorial shuffling of polypeptide segments
    • Riechmann L., and Winter G. Novel folded protein domains generated by combinatorial shuffling of polypeptide segments. Proc. Natl Acad. Sci. USA 97 (2000) 10068-10073
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10068-10073
    • Riechmann, L.1    Winter, G.2
  • 5
    • 0842291810 scopus 로고    scopus 로고
    • A native-like artificial protein from anti-sense DNA
    • Fischer N., Riechmann L., and Winter G. A native-like artificial protein from anti-sense DNA. Protein Eng. Des. Sel. 17 (2004) 13-20
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 13-20
    • Fischer, N.1    Riechmann, L.2    Winter, G.3
  • 8
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 9
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem. Sci. 27 (2002) 527-533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 10
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe A.D., and Szostak J.W. Functional proteins from a random-sequence library. Nature 410 (2001) 715-718
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 11
    • 33644851164 scopus 로고    scopus 로고
    • Fancy footwork in the sequence space shuffle
    • Arnold F.H. Fancy footwork in the sequence space shuffle. Nature Biotechnol. 24 (2006) 328-330
    • (2006) Nature Biotechnol. , vol.24 , pp. 328-330
    • Arnold, F.H.1
  • 12
    • 0000099196 scopus 로고
    • The structure of hen egg white lysozyme: a three dimensional Fourier synthesis at 2 Å resolution
    • Blake C.C.F., Koenig D.F., Mair G.A., North A.C., Phillips D.C., and Sarma V.R. The structure of hen egg white lysozyme: a three dimensional Fourier synthesis at 2 Å resolution. Nature 196 (1965) 1173-1176
    • (1965) Nature , vol.196 , pp. 1173-1176
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.4    Phillips, D.C.5    Sarma, V.R.6
  • 13
    • 0013971370 scopus 로고
    • The three-dimensional structure of an enzyme molecule
    • Phillips D.C. The three-dimensional structure of an enzyme molecule. Sci. Am. 215 (1966) 78-90
    • (1966) Sci. Am. , vol.215 , pp. 78-90
    • Phillips, D.C.1
  • 15
    • 0035940959 scopus 로고    scopus 로고
    • Cooperative folding of the isolated alpha-helical domain of hen egg-white lysozyme
    • Bai P., and Peng Z.Y. Cooperative folding of the isolated alpha-helical domain of hen egg-white lysozyme. J. Mol Biol. 314 (2001) 321-329
    • (2001) J. Mol Biol. , vol.314 , pp. 321-329
    • Bai, P.1    Peng, Z.Y.2
  • 17
    • 22844444097 scopus 로고    scopus 로고
    • Water molecules in the antibody-antigen interface of the structure of the Fab HyHEL-5-lysozyme complex at 1.7 Å resolution: comparison with results from isothermal titration calorimetry
    • Cohen G.H., Silverton E.W., Padlan E.A., Dyda F., Wibbenmeyer J.A., Willson R.C., and Davies D.R. Water molecules in the antibody-antigen interface of the structure of the Fab HyHEL-5-lysozyme complex at 1.7 Å resolution: comparison with results from isothermal titration calorimetry. Acta Crystallog. sect. D 61 (2005) 628-633
    • (2005) Acta Crystallog. sect. D , vol.61 , pp. 628-633
    • Cohen, G.H.1    Silverton, E.W.2    Padlan, E.A.3    Dyda, F.4    Wibbenmeyer, J.A.5    Willson, R.C.6    Davies, D.R.7
  • 18
    • 0027971497 scopus 로고
    • Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1
    • Braden B.C., Souchon H., Eisele J.L., Bentley G.A., Bhat T.N., Navaza J., and Poljak R.J. Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1. J. Mol. Biol. 243 (1994) 767-781
    • (1994) J. Mol. Biol. , vol.243 , pp. 767-781
    • Braden, B.C.1    Souchon, H.2    Eisele, J.L.3    Bentley, G.A.4    Bhat, T.N.5    Navaza, J.6    Poljak, R.J.7
  • 19
    • 0033563266 scopus 로고    scopus 로고
    • Lack of significant differences in association rates and affinities of antibodies from short-term and long-term responses to hen egg lysozyme
    • Goldbaum F.A., Cauerhff A., Velikovsky C.A., Llera A.S., Riottot M.M., and Poljak R.J. Lack of significant differences in association rates and affinities of antibodies from short-term and long-term responses to hen egg lysozyme. J. Immunol. 162 (1999) 6040-6045
    • (1999) J. Immunol. , vol.162 , pp. 6040-6045
    • Goldbaum, F.A.1    Cauerhff, A.2    Velikovsky, C.A.3    Llera, A.S.4    Riottot, M.M.5    Poljak, R.J.6
  • 20
    • 0031919676 scopus 로고
    • Association and dissociation kinetics of anti-hen egg lysozyme monoclonal antibodies HyHEL5 and HyHEL10
    • Xavier K.A., and Willson R.C. Association and dissociation kinetics of anti-hen egg lysozyme monoclonal antibodies HyHEL5 and HyHEL10. Biophys. J. 74 (1993) 2036-2045
    • (1993) Biophys. J. , vol.74 , pp. 2036-2045
    • Xavier, K.A.1    Willson, R.C.2
  • 23
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • Schulz H., Hennecke H., and Thöny-Meyer L. Prototype of a heme chaperone essential for cytochrome c maturation. Science 281 (1998) 1197-1200
    • (1998) Science , vol.281 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thöny-Meyer, L.3
  • 24
    • 0037162447 scopus 로고    scopus 로고
    • The CcmE protein of the c-type cytochrome biogenesis system: unusual in vitro heme incorporation into apo-CcmE and transfer from holo-CcmE to apocytochrome
    • Daltrop O., Stevens J.M., Higham C.W., and Ferguson S.J. The CcmE protein of the c-type cytochrome biogenesis system: unusual in vitro heme incorporation into apo-CcmE and transfer from holo-CcmE to apocytochrome. Proc. Natl Acad. Sci. USA 99 (2002) 9703-9708
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9703-9708
    • Daltrop, O.1    Stevens, J.M.2    Higham, C.W.3    Ferguson, S.J.4
  • 25
    • 1542298190 scopus 로고    scopus 로고
    • Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystissp. PCC 6803 and Synechococcus sp. PCC 7002
    • Vu B.C., Vuletich D.A., Kuriakose S.A., Falzone C.J., and Lecomte J.T.J. Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystissp. PCC 6803 and Synechococcus sp. PCC 7002. J. Biol. Inorg. Chem. 9 (2004) 183-194
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 183-194
    • Vu, B.C.1    Vuletich, D.A.2    Kuriakose, S.A.3    Falzone, C.J.4    Lecomte, J.T.J.5
  • 26
    • 0034697020 scopus 로고    scopus 로고
    • X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution
    • Fiedler T.J., Davey C.A., and Fenna R.E. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution. J. Biol. Chem. 275 (2000) 11964-11971
    • (2000) J. Biol. Chem. , vol.275 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fenna, R.E.3
  • 27
    • 0037066698 scopus 로고    scopus 로고
    • Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family
    • LeBrun L.A., Hoch U., and de Montellano P.R.O. Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family. J. Biol. Chem. 277 (2002) 12755-12761
    • (2002) J. Biol. Chem. , vol.277 , pp. 12755-12761
    • LeBrun, L.A.1    Hoch, U.2    de Montellano, P.R.O.3
  • 28
    • 0036005637 scopus 로고    scopus 로고
    • Role of cofactors in protein folding
    • Wittung-Stafshede P. Role of cofactors in protein folding. Accs Chem. Res. 35 (2002) 201-208
    • (2002) Accs Chem. Res. , vol.35 , pp. 201-208
    • Wittung-Stafshede, P.1
  • 32
    • 0034646996 scopus 로고    scopus 로고
    • The outcome of acute hepatitis C predicted by the evolution of the viral quasispecies
    • Farci P., Shimoda A., Coiana A., Diaz G., Peddis G., Melpolder J.C., et al. The outcome of acute hepatitis C predicted by the evolution of the viral quasispecies. Science 288 (2000) 339-344
    • (2000) Science , vol.288 , pp. 339-344
    • Farci, P.1    Shimoda, A.2    Coiana, A.3    Diaz, G.4    Peddis, G.5    Melpolder, J.C.6
  • 33
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong P.D., Doyle M.L., Casper D.J., Cicala C., Leavitt S.A., Majeed S., et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 420 (2002) 678-682
    • (2002) Nature , vol.420 , pp. 678-682
    • Kwong, P.D.1    Doyle, M.L.2    Casper, D.J.3    Cicala, C.4    Leavitt, S.A.5    Majeed, S.6
  • 34
    • 0032100706 scopus 로고    scopus 로고
    • Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate
    • Batista F.D., and Neuberger M.S. Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate. Immunity 8 (1998) 751-759
    • (1998) Immunity , vol.8 , pp. 751-759
    • Batista, F.D.1    Neuberger, M.S.2
  • 35
    • 0005229135 scopus 로고    scopus 로고
    • Mimicking somatic hypermutation: affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain
    • Low N.M., Holliger P.H., and Winter G. Mimicking somatic hypermutation: affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain. J. Mol. Biol. 260 (1996) 359-368
    • (1996) J. Mol. Biol. , vol.260 , pp. 359-368
    • Low, N.M.1    Holliger, P.H.2    Winter, G.3
  • 37
    • 0033868957 scopus 로고    scopus 로고
    • Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of Mpd
    • Weiss M.S., Palm G.J., and Hilgenfeld R. Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of Mpd. Acta Crystallog. sect. D 56 (2000) 952-958
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 952-958
    • Weiss, M.S.1    Palm, G.J.2    Hilgenfeld, R.3
  • 38
    • 0035854744 scopus 로고    scopus 로고
    • Structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 angstroms: insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase
    • Singh S.K., Matsuno K., Laporte D.C., and Banaszak L.J. Structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 angstroms: insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase. J. Biol. Chem. 276 (2001) 26154-26163
    • (2001) J. Biol. Chem. , vol.276 , pp. 26154-26163
    • Singh, S.K.1    Matsuno, K.2    Laporte, D.C.3    Banaszak, L.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.