메뉴 건너뛰기




Volumn 404, Issue 2, 2010, Pages 307-327

Design, Production and Molecular Structure of a New Family of Artificial Alpha-helicoidal Repeat Proteins (αRep) Based on Thermostable HEAT-like Repeats

Author keywords

Combinatorial library; HEAT repeat protein; Protein design; Protein scaffold

Indexed keywords

ALPHA HELICOIDAL REPEAT PROTEIN; DIMER; TETRATRICOPEPTIDE REPEAT PROTEIN; UNCLASSIFIED DRUG;

EID: 78349304669     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.048     Document Type: Article
Times cited : (82)

References (53)
  • 1
    • 34548522063 scopus 로고    scopus 로고
    • Alternative non-antibody scaffolds for molecular recognition
    • Skerra A. Alternative non-antibody scaffolds for molecular recognition. Curr. Opin. Biotechnol. 2007, 18:295-304.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 295-304
    • Skerra, A.1
  • 2
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz H.K., Amstutz P., Pluckthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat. Biotechnol. 2005, 23:1257-1268.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 3
    • 23644452792 scopus 로고    scopus 로고
    • Engineered proteins as specific binding reagents
    • Binz H.K., Pluckthun A. Engineered proteins as specific binding reagents. Curr. Opin. Biotechnol. 2005, 16:459-469.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 459-469
    • Binz, H.K.1    Pluckthun, A.2
  • 4
    • 43549101411 scopus 로고    scopus 로고
    • Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold
    • Nygren P.A. Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold. FEBS J. 2008, 275:2668-2676.
    • (2008) FEBS J. , vol.275 , pp. 2668-2676
    • Nygren, P.A.1
  • 5
    • 34547457742 scopus 로고    scopus 로고
    • Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain
    • Koide A., Koide S. Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain. Methods Mol. Biol. 2007, 352:95-109.
    • (2007) Methods Mol. Biol. , vol.352 , pp. 95-109
    • Koide, A.1    Koide, S.2
  • 6
    • 27644540066 scopus 로고    scopus 로고
    • Anticalins as an alternative to antibody technology
    • Schlehuber S., Skerra A. Anticalins as an alternative to antibody technology. Expert Opin. Biol. Ther. 2005, 5:1453-1462.
    • (2005) Expert Opin. Biol. Ther. , vol.5 , pp. 1453-1462
    • Schlehuber, S.1    Skerra, A.2
  • 7
    • 34547663529 scopus 로고    scopus 로고
    • Affilin-novel binding molecules based on human gamma-B-crystallin, an all beta-sheet protein
    • Ebersbach H., Fiedler E., Scheuermann T., Fiedler M., Stubbs M.T., Reimann C., et al. Affilin-novel binding molecules based on human gamma-B-crystallin, an all beta-sheet protein. J. Mol. Biol. 2007, 372:172-185.
    • (2007) J. Mol. Biol. , vol.372 , pp. 172-185
    • Ebersbach, H.1    Fiedler, E.2    Scheuermann, T.3    Fiedler, M.4    Stubbs, M.T.5    Reimann, C.6
  • 8
    • 33646519459 scopus 로고    scopus 로고
    • Structures of in vitro evolved binding sites on neocarzinostatin scaffold reveal unanticipated evolutionary pathways
    • Drevelle A., Graille M., Heyd B., Sorel I., Ulryck N., Pecorari F., et al. Structures of in vitro evolved binding sites on neocarzinostatin scaffold reveal unanticipated evolutionary pathways. J. Mol. Biol. 2006, 358:455-471.
    • (2006) J. Mol. Biol. , vol.358 , pp. 455-471
    • Drevelle, A.1    Graille, M.2    Heyd, B.3    Sorel, I.4    Ulryck, N.5    Pecorari, F.6
  • 9
    • 0038290448 scopus 로고    scopus 로고
    • In vitro evolution of the binding specificity of neocarzinostatin, an enediyne-binding chromoprotein
    • Heyd B., Pecorari F., Collinet B., Adjadj E., Desmadril M., Minard P. In vitro evolution of the binding specificity of neocarzinostatin, an enediyne-binding chromoprotein. Biochemistry 2003, 42:5674-5683.
    • (2003) Biochemistry , vol.42 , pp. 5674-5683
    • Heyd, B.1    Pecorari, F.2    Collinet, B.3    Adjadj, E.4    Desmadril, M.5    Minard, P.6
  • 10
    • 67651152812 scopus 로고    scopus 로고
    • Disulfide bond substitution by directed evolution in an engineered binding protein
    • Drevelle A., Urvoas A., Hamida-Rebai M.B., Van Vooren G., Nicaise M., et al. Disulfide bond substitution by directed evolution in an engineered binding protein. ChemBiochem 2009, 10:1349-1359.
    • (2009) ChemBiochem , vol.10 , pp. 1349-1359
    • Drevelle, A.1    Urvoas, A.2    Hamida-Rebai, M.B.3    Van Vooren, G.4    Nicaise, M.5
  • 11
    • 0037468685 scopus 로고    scopus 로고
    • A novel strategy to design binding molecules harnessing the modular nature of repeat proteins
    • Forrer P., Stumpp M.T., Binz H.K., Pluckthun A. A novel strategy to design binding molecules harnessing the modular nature of repeat proteins. FEBS Lett. 2003, 539:2-6.
    • (2003) FEBS Lett. , vol.539 , pp. 2-6
    • Forrer, P.1    Stumpp, M.T.2    Binz, H.K.3    Pluckthun, A.4
  • 13
    • 0035783062 scopus 로고    scopus 로고
    • Review: proteins with repeated sequence - structural prediction and modeling
    • Kajava A.V. Review: proteins with repeated sequence - structural prediction and modeling. J. Struct. Biol. 2001, 134:132-144.
    • (2001) J. Struct. Biol. , vol.134 , pp. 132-144
    • Kajava, A.V.1
  • 14
    • 32944477673 scopus 로고    scopus 로고
    • The evolution of adaptive immunity
    • Pancer Z., Cooper M.D. The evolution of adaptive immunity. Annu. Rev. Immunol. 2006, 24:497-518.
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 497-518
    • Pancer, Z.1    Cooper, M.D.2
  • 15
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz H.K., Stumpp M.T., Forrer P., Amstutz P., Pluckthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 2003, 332:489-503.
    • (2003) J. Mol. Biol. , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Pluckthun, A.5
  • 16
    • 18744380008 scopus 로고    scopus 로고
    • Consensus-derived structural determinants of the ankyrin repeat motif
    • Mosavi L.K., Minor D.L., Peng Z.Y. Consensus-derived structural determinants of the ankyrin repeat motif. Proc. Natl Acad. Sci. USA 2002, 99:16029-16034.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16029-16034
    • Mosavi, L.K.1    Minor, D.L.2    Peng, Z.Y.3
  • 17
    • 2342624119 scopus 로고    scopus 로고
    • High-affinity binders selected from designed ankyrin repeat protein libraries
    • Binz H.K., Amstutz P., Kohl A., Stumpp M.T., Briand C., Forrer P., et al. High-affinity binders selected from designed ankyrin repeat protein libraries. Nat. Biotechnol. 2004, 22:575-582.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 575-582
    • Binz, H.K.1    Amstutz, P.2    Kohl, A.3    Stumpp, M.T.4    Briand, C.5    Forrer, P.6
  • 18
    • 34247853389 scopus 로고    scopus 로고
    • Inhibition of caspase-2 by a designed ankyrin repeat protein: specificity, structure, and inhibition mechanism
    • Schweizer A., Roschitzki-Voser H., Amstutz P., Briand C., Gulotti-Georgieva M., Prenosil E., et al. Inhibition of caspase-2 by a designed ankyrin repeat protein: specificity, structure, and inhibition mechanism. Structure 2007, 15:625-636.
    • (2007) Structure , vol.15 , pp. 625-636
    • Schweizer, A.1    Roschitzki-Voser, H.2    Amstutz, P.3    Briand, C.4    Gulotti-Georgieva, M.5    Prenosil, E.6
  • 20
    • 0043281585 scopus 로고    scopus 로고
    • Designing repeat proteins: modular leucine-rich repeat protein libraries based on the mammalian ribonuclease inhibitor family
    • Stumpp M.T., Forrer P., Binz H.K., Pluckthun A. Designing repeat proteins: modular leucine-rich repeat protein libraries based on the mammalian ribonuclease inhibitor family. J. Mol. Biol 2003, 332:471-487.
    • (2003) J. Mol. Biol , vol.332 , pp. 471-487
    • Stumpp, M.T.1    Forrer, P.2    Binz, H.K.3    Pluckthun, A.4
  • 21
    • 17644425688 scopus 로고    scopus 로고
    • Local and long-range stability in tandemly arrayed tetratricopeptide repeats
    • Main E.R., Stott K., Jackson S.E., Regan L. Local and long-range stability in tandemly arrayed tetratricopeptide repeats. Proc. Natl Acad. Sci. USA 2005, 102:5721-5726.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5721-5726
    • Main, E.R.1    Stott, K.2    Jackson, S.E.3    Regan, L.4
  • 23
    • 77953816068 scopus 로고    scopus 로고
    • Screening libraries to identify proteins with desired binding activities using a split-GFP reassembly assay
    • Jackrel M.E., Cortajarena A.L., Liu T.Y., Regan L. Screening libraries to identify proteins with desired binding activities using a split-GFP reassembly assay. ACS Chem. Biol. 2010, 5:553-562.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 553-562
    • Jackrel, M.E.1    Cortajarena, A.L.2    Liu, T.Y.3    Regan, L.4
  • 24
    • 42449136263 scopus 로고    scopus 로고
    • Designed TPR modules as novel anticancer agents
    • Cortajarena A.L., Yi F., Regan L. Designed TPR modules as novel anticancer agents. ACS Chem. Biol. 2008, 3:161-166.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 161-166
    • Cortajarena, A.L.1    Yi, F.2    Regan, L.3
  • 25
    • 39149098445 scopus 로고    scopus 로고
    • Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core
    • Parmeggiani F., Pellarin R., Larsen A.P., Varadamsetty G., Stumpp M.T., Zerbe O., et al. Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core. J. Mol. Biol. 2008, 376:1282-1304.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1282-1304
    • Parmeggiani, F.1    Pellarin, R.2    Larsen, A.P.3    Varadamsetty, G.4    Stumpp, M.T.5    Zerbe, O.6
  • 27
    • 70349512813 scopus 로고    scopus 로고
    • Highly sensitive detection of individual HEAT and ARM repeats with HHpred and COACH
    • Kippert F., Gerloff D.L. Highly sensitive detection of individual HEAT and ARM repeats with HHpred and COACH. PLoS One 2009, 4:e7148.
    • (2009) PLoS One , vol.4
    • Kippert, F.1    Gerloff, D.L.2
  • 29
    • 0034830935 scopus 로고    scopus 로고
    • Rapid amplification of plasmid and phage DNA using Phi 29 DNA polymerase and multiply-primed rolling circle amplification
    • Dean F.B., Nelson J.R., Giesler T.L., Lasken R.S. Rapid amplification of plasmid and phage DNA using Phi 29 DNA polymerase and multiply-primed rolling circle amplification. Genome Res. 2001, 11:1095-1099.
    • (2001) Genome Res. , vol.11 , pp. 1095-1099
    • Dean, F.B.1    Nelson, J.R.2    Giesler, T.L.3    Lasken, R.S.4
  • 30
    • 34250665073 scopus 로고    scopus 로고
    • Colony filtration blotting for screening soluble expression in Escherichia coli
    • Dahlroth S.L., Nordlund P., Cornvik T. Colony filtration blotting for screening soluble expression in Escherichia coli. Nat. Protoc. 2006, 1:253-258.
    • (2006) Nat. Protoc. , vol.1 , pp. 253-258
    • Dahlroth, S.L.1    Nordlund, P.2    Cornvik, T.3
  • 32
    • 33746161571 scopus 로고    scopus 로고
    • Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display
    • Steiner D., Forrer P., Stumpp M.T., Pluckthun A. Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display. Nat. Biotechnol. 2006, 24:823-831.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 823-831
    • Steiner, D.1    Forrer, P.2    Stumpp, M.T.3    Pluckthun, A.4
  • 33
    • 0037147328 scopus 로고    scopus 로고
    • What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome
    • Kajava A.V. What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome. J. Biol. Chem. 2002, 277:49791-49798.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49791-49798
    • Kajava, A.V.1
  • 34
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., Koch M.H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 2001, 80:2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 36
    • 4744365127 scopus 로고    scopus 로고
    • Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif
    • Magliery T.J., Regan L. Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif. J. Mol. Biol. 2004, 343:731-745.
    • (2004) J. Mol. Biol. , vol.343 , pp. 731-745
    • Magliery, T.J.1    Regan, L.2
  • 37
    • 3242790224 scopus 로고    scopus 로고
    • Selection of internalizing ligand-display phage using rolling circle amplification for phage recovery
    • Burg M., Ravey E.P., Gonzales M., Amburn E., Faix P.H., Baird A., Larocca D. Selection of internalizing ligand-display phage using rolling circle amplification for phage recovery. DNA Cell Biol. 2004, 23:457-462.
    • (2004) DNA Cell Biol. , vol.23 , pp. 457-462
    • Burg, M.1    Ravey, E.P.2    Gonzales, M.3    Amburn, E.4    Faix, P.H.5    Baird, A.6    Larocca, D.7
  • 38
    • 33750009895 scopus 로고    scopus 로고
    • Tapping diversity lost in transformations - in vitro amplification of ligation reactions
    • Christ D., Famm K., Winter G. Tapping diversity lost in transformations - in vitro amplification of ligation reactions. Nucleic Acids Res. 2006, 34:e108.
    • (2006) Nucleic Acids Res. , vol.34
    • Christ, D.1    Famm, K.2    Winter, G.3
  • 40
    • 51349091340 scopus 로고    scopus 로고
    • Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display
    • Steiner D., Forrer P., Pluckthun A. Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display. J. Mol. Biol. 2008, 382:1211-1227.
    • (2008) J. Mol. Biol. , vol.382 , pp. 1211-1227
    • Steiner, D.1    Forrer, P.2    Pluckthun, A.3
  • 41
    • 0000625192 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. Acta Crystallogr. D 1993, 50:760-763.
    • (1993) Acta Crystallogr. D , vol.50 , pp. 760-763
    • Kabsch, W.1
  • 43
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0
    • Bricogne G., Vonrhein C., Flensburg C., Schiltz M., Paciorek W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D 2003, 59:2023-2030.
    • (2003) Acta Crystallogr. D , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 46
    • 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. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 47
    • 70349316826 scopus 로고    scopus 로고
    • Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments a the Synchrotron SOLEIL SWING beamline
    • David G., Pérez J. Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments a the Synchrotron SOLEIL SWING beamline. J. Appl. Crystallogr 2009, 42:892-900.
    • (2009) J. Appl. Crystallogr , vol.42 , pp. 892-900
    • David, G.1    Pérez, J.2
  • 50
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 1992, 25:495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 51
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modelling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., Svergun D.I. Global rigid body modelling of macromolecular complexes against small-angle scattering data. Biophys. J. 2005.
    • (2005) Biophys. J.
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 52
    • 33747819887 scopus 로고    scopus 로고
    • SABBAC: online structural alphabet-based protein backbone reconstruction from alpha-carbon trace
    • Maupetit J., Gautier R., Tuffery P. SABBAC: online structural alphabet-based protein backbone reconstruction from alpha-carbon trace. Nucleic Acids Res. 2006, 34:W147-W151.
    • (2006) Nucleic Acids Res. , vol.34
    • Maupetit, J.1    Gautier, R.2    Tuffery, P.3
  • 53
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 1995, 28:768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.