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Volumn 404, Issue 3, 2010, Pages 381-391

Structural determinants for improved stability of designed ankyrin repeat proteins with a redesigned C-Capping Module

Author keywords

Ankyrin repeat; Crystal structure; Protein engineering; Protein recognition; Thermodynamic stability

Indexed keywords

AMINO ACID; ANKYRIN; BINDING PROTEIN; DESIGNED ANKYRIN REPEAT PROTEIN; UNCLASSIFIED DRUG;

EID: 78349313323     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.023     Document Type: Article
Times cited : (69)

References (31)
  • 2
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?
    • Bork P. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?. Proteins 1993, 17:363-374.
    • (1993) Proteins , vol.17 , pp. 363-374
    • Bork, P.1
  • 3
    • 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
  • 4
    • 0037648552 scopus 로고    scopus 로고
    • Design of stable alpha-helical arrays from an idealized TPR motif
    • Main E.R., Xiong Y., Cocco M.J., D'Andrea L., Regan L. Design of stable alpha-helical arrays from an idealized TPR motif. Structure 2003, 11:497-508.
    • (2003) Structure , vol.11 , pp. 497-508
    • Main, E.R.1    Xiong, Y.2    Cocco, M.J.3    D'Andrea, L.4    Regan, L.5
  • 5
    • 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., Plückthun 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    Plückthun, A.4
  • 6
    • 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
  • 7
    • 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., Plückthun 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    Plückthun, A.5
  • 8
    • 38049063892 scopus 로고    scopus 로고
    • Folding and unfolding mechanism of highly stable full-consensus ankyrin repeat proteins
    • Wetzel S.K., Settanni G., Kenig M., Binz H.K., Plückthun A. Folding and unfolding mechanism of highly stable full-consensus ankyrin repeat proteins. J. Mol. Biol. 2008, 376:241-257.
    • (2008) J. Mol. Biol. , vol.376 , pp. 241-257
    • Wetzel, S.K.1    Settanni, G.2    Kenig, M.3    Binz, H.K.4    Plückthun, A.5
  • 9
    • 0344874146 scopus 로고    scopus 로고
    • Structure-based substitutions for increased solubility of a designed protein
    • Mosavi L.K., Peng Z.Y. Structure-based substitutions for increased solubility of a designed protein. Protein Eng. 2003, 16:739-745.
    • (2003) Protein Eng. , vol.16 , pp. 739-745
    • Mosavi, L.K.1    Peng, Z.Y.2
  • 10
    • 37349036497 scopus 로고    scopus 로고
    • Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments
    • Interlandi G., Wetzel S.K., Settanni G., Plückthun A., Caflisch A. Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments. J. Mol. Biol. 2008, 375:837-854.
    • (2008) J. Mol. Biol. , vol.375 , pp. 837-854
    • Interlandi, G.1    Wetzel, S.K.2    Settanni, G.3    Plückthun, A.4    Caflisch, A.5
  • 11
    • 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
  • 12
    • 51349091340 scopus 로고    scopus 로고
    • Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display
    • Steiner D., Forrer P., Plückthun 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    Plückthun, A.3
  • 14
    • 21744440783 scopus 로고    scopus 로고
    • Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins
    • Amstutz P., Binz H.K., Parizek P., Stumpp M.T., Kohl A., Grütter M.G., et al. Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins. J. Biol. Chem. 2005, 280:24715-24722.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24715-24722
    • Amstutz, P.1    Binz, H.K.2    Parizek, P.3    Stumpp, M.T.4    Kohl, A.5    Grütter, M.G.6
  • 15
    • 23444448571 scopus 로고    scopus 로고
    • Allosteric inhibition of aminoglycoside phosphotransferase by a designed ankyrin repeat protein
    • Kohl A., Amstutz P., Parizek P., Binz H.K., Briand C., Capitani G., et al. Allosteric inhibition of aminoglycoside phosphotransferase by a designed ankyrin repeat protein. Structure 2005, 13:1131-1141.
    • (2005) Structure , vol.13 , pp. 1131-1141
    • Kohl, A.1    Amstutz, P.2    Parizek, P.3    Binz, H.K.4    Briand, C.5    Capitani, G.6
  • 17
    • 33749002845 scopus 로고    scopus 로고
    • Molecular dynamics study of the stabilities of consensus designed ankyrin repeat proteins
    • Yu H., Kohl A., Binz H.K., Plückthun A., Grütter M.G., van Gunsteren W.F. Molecular dynamics study of the stabilities of consensus designed ankyrin repeat proteins. Proteins 2006, 65:285-295.
    • (2006) Proteins , vol.65 , pp. 285-295
    • Yu, H.1    Kohl, A.2    Binz, H.K.3    Plückthun, A.4    Grütter, M.G.5    van Gunsteren, W.F.6
  • 18
    • 33749001195 scopus 로고    scopus 로고
    • Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability
    • Binz H.K., Kohl A., Plückthun A., Grütter M.G. Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability. Proteins 2006, 65:280-284.
    • (2006) Proteins , vol.65 , pp. 280-284
    • Binz, H.K.1    Kohl, A.2    Plückthun, A.3    Grütter, M.G.4
  • 19
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M.C., Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 1993, 234:946-950.
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 22
    • 77956176007 scopus 로고    scopus 로고
    • Residue-resolved stability of full-consensus ankyrin repeat proteins probed by NMR
    • Wetzel S.K., Ewald C., Settanni G., Jurt S., Plückthun A., Zerbe O. Residue-resolved stability of full-consensus ankyrin repeat proteins probed by NMR. J. Mol. Biol. 2010, 402:241-258.
    • (2010) J. Mol. Biol. , vol.402 , pp. 241-258
    • Wetzel, S.K.1    Ewald, C.2    Settanni, G.3    Jurt, S.4    Plückthun, A.5    Zerbe, O.6
  • 23
    • 0027879008 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. J. Appl. Crystallogr. 1993, 26:795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 27
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • Yeates T.O. Detecting and overcoming crystal twinning. Methods Enzymol. 1997, 276:344-358.
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 30
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 1993, 231:1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.