메뉴 건너뛰기




Volumn 16, Issue 10, 2008, Pages 1443-1453

Chaperone-Assisted Crystallography with DARPins

Author keywords

PROTEINS

Indexed keywords

ANTIBODY; ANTIGEN; CASPASE 2; CASPASE INHIBITOR; CHAPERONE; DESIGN ANKYRIN REPEAT PROTEIN; MALTOSE BINDING PROTEIN; MEMBRANE PROTEIN; PHOSPHOTRANSFERASE; POLO LIKE KINASE 1; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 53049085400     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.08.010     Document Type: Review
Times cited : (69)

References (58)
  • 1
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution
    • Amit A.G., Mariuzza R.A., Phillips S.E., and Poljak R.J. Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution. Science 233 (1986) 747-753
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.3    Poljak, R.J.4
  • 3
    • 0004253967 scopus 로고
    • Cocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operator
    • Anderson J., Ptashne M., and Harrison S.C. Cocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operator. Proc. Natl. Acad. Sci. USA 81 (1984) 1307-1311
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1307-1311
    • Anderson, J.1    Ptashne, M.2    Harrison, S.C.3
  • 5
    • 0032512459 scopus 로고    scopus 로고
    • The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA
    • Batchelor A.H., Piper D.E., de la Brousse F.C., McKnight S.L., and Wolberger C. The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA. Science 279 (1998) 1037-1041
    • (1998) Science , vol.279 , pp. 1037-1041
    • Batchelor, A.H.1    Piper, D.E.2    de la Brousse, F.C.3    McKnight, S.L.4    Wolberger, C.5
  • 6
    • 0029689665 scopus 로고    scopus 로고
    • The crystal structures of complexes formed between lysozyme and antibody fragments
    • Bentley G.A. The crystal structures of complexes formed between lysozyme and antibody fragments. EXS 75 (1996) 301-319
    • (1996) EXS , vol.75 , pp. 301-319
    • Bentley, G.A.1
  • 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., and Plückthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 332 (2003) 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
  • 9
    • 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 17 (1993) 363-374
    • (1993) Proteins , vol.17 , pp. 363-374
    • Bork, P.1
  • 11
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies D.R., and Cohen G.H. Interactions of protein antigens with antibodies. Proc. Natl. Acad. Sci. USA 93 (1996) 7-12
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 13
    • 4344698577 scopus 로고    scopus 로고
    • The use of recombinant methods and molecular engineering in protein crystallization
    • Derewenda Z.S. The use of recombinant methods and molecular engineering in protein crystallization. Methods 34 (2004) 354-363
    • (2004) Methods , vol.34 , pp. 354-363
    • Derewenda, Z.S.1
  • 16
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler R., Campbell E.B., and MacKinnon R. Gating the selectivity filter in ClC chloride channels. Science 300 (2003) 108-112
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 17
    • 4344714933 scopus 로고    scopus 로고
    • Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition
    • Fellouse F.A., Wiesmann C., and Sidhu S.S. Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition. Proc. Natl. Acad. Sci. USA 101 (2004) 12467-12472
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12467-12472
    • Fellouse, F.A.1    Wiesmann, C.2    Sidhu, S.S.3
  • 20
    • 33751347582 scopus 로고    scopus 로고
    • Biopharmaceutical drug discovery using novel protein scaffolds
    • Gill D.S., and Damle N.K. Biopharmaceutical drug discovery using novel protein scaffolds. Curr. Opin. Biotechnol. 17 (2006) 653-658
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 653-658
    • Gill, D.S.1    Damle, N.K.2
  • 21
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J., and Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. USA 94 (1997) 4937-4942
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 22
  • 23
    • 0030830868 scopus 로고    scopus 로고
    • Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases
    • Hon W.C., McKay G.A., Thompson P.R., Sweet R.M., Yang D.S., Wright G.D., and Berghuis A.M. Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell 89 (1997) 887-895
    • (1997) Cell , vol.89 , pp. 887-895
    • Hon, W.C.1    McKay, G.A.2    Thompson, P.R.3    Sweet, R.M.4    Yang, D.S.5    Wright, G.D.6    Berghuis, A.M.7
  • 24
    • 0036667741 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins mediated by antibody fragments
    • Hunte C., and Michel H. Crystallisation of membrane proteins mediated by antibody fragments. Curr. Opin. Struct. Biol. 12 (2002) 503-508
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 503-508
    • Hunte, C.1    Michel, H.2
  • 25
    • 0034660152 scopus 로고    scopus 로고
    • Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • Hunte C., Koepke J., Lange C., Rossmanith T., and Michel H. Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8 (2000) 669-684
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 26
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation
    • Huxford T., Huang D.B., Malek S., and Ghosh G. The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. Cell 95 (1998) 759-770
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 27
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (1995) 660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 28
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IkappaBalpha/NF-kappaB complex
    • Jacobs M.D., and Harrison S.C. Structure of an IkappaBalpha/NF-kappaB complex. Cell 95 (1998) 749-758
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 29
    • 0034671563 scopus 로고    scopus 로고
    • Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors
    • Jeffrey P.D., Tong L., and Pavletich N.P. Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors. Genes Dev. 14 (2000) 3115-3125
    • (2000) Genes Dev. , vol.14 , pp. 3115-3125
    • Jeffrey, P.D.1    Tong, L.2    Pavletich, N.P.3
  • 30
  • 34
    • 0028294931 scopus 로고
    • Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex
    • Kortt A.A., Malby R.L., Caldwell J.B., Gruen L.C., Ivancic N., Lawrence M.C., Howlett G.J., Webster R.G., Hudson P.J., and Colman P.M. Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex. Eur. J. Biochem. 221 (1994) 151-157
    • (1994) Eur. J. Biochem. , vol.221 , pp. 151-157
    • Kortt, A.A.1    Malby, R.L.2    Caldwell, J.B.3    Gruen, L.C.4    Ivancic, N.5    Lawrence, M.C.6    Howlett, G.J.7    Webster, R.G.8    Hudson, P.J.9    Colman, P.M.10
  • 36
    • 0025351555 scopus 로고
    • Epitopes on protein antigens: misconceptions and realities
    • Laver W.G., Air G.M., Webster R.G., and Smith-Gill S.J. Epitopes on protein antigens: misconceptions and realities. Cell 61 (1990) 553-556
    • (1990) Cell , vol.61 , pp. 553-556
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3    Smith-Gill, S.J.4
  • 38
    • 0037482136 scopus 로고    scopus 로고
    • X-ray crystal structure of an IkappaBbeta x NF-kappaB p65 homodimer complex
    • Malek S., Huang D.B., Huxford T., Ghosh S., and Ghosh G. X-ray crystal structure of an IkappaBbeta x NF-kappaB p65 homodimer complex. J. Biol. Chem. 278 (2003) 23094-23100
    • (2003) J. Biol. Chem. , vol.278 , pp. 23094-23100
    • Malek, S.1    Huang, D.B.2    Huxford, T.3    Ghosh, S.4    Ghosh, G.5
  • 39
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S., Nakashima R., Yamashita E., and Yamaguchi A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419 (2002) 587-593
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 40
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • Murakami S., Nakashima R., Yamashita E., Matsumoto T., and Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443 (2006) 173-179
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 43
    • 0028991525 scopus 로고
    • Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase
    • Ostermeier C., Iwata S., Ludwig B., and Michel H. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nat. Struct. Biol. 2 (1995) 842-846
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 842-846
    • Ostermeier, C.1    Iwata, S.2    Ludwig, B.3    Michel, H.4
  • 44
    • 0025275610 scopus 로고
    • On the nature of antibody combining sites: unusual structural features that may confer on these sites an enhanced capacity for binding ligands
    • Padlan E.A. On the nature of antibody combining sites: unusual structural features that may confer on these sites an enhanced capacity for binding ligands. Proteins 7 (1990) 112-124
    • (1990) Proteins , vol.7 , pp. 112-124
    • Padlan, E.A.1
  • 45
    • 39149087988 scopus 로고    scopus 로고
    • The human combinatorial antibody library HuCAL GOLD combines diversification of all six CDRs according to the natural immune system with a novel display method for efficient selection of high-affinity antibodies
    • Rothe C., Urlinger S., Lohning C., Prassler J., Stark Y., Jager U., Hubner B., Bardroff M., Pradel I., Boss M., et al. The human combinatorial antibody library HuCAL GOLD combines diversification of all six CDRs according to the natural immune system with a novel display method for efficient selection of high-affinity antibodies. J. Mol. Biol. 376 (2008) 1182-1200
    • (2008) J. Mol. Biol. , vol.376 , pp. 1182-1200
    • Rothe, C.1    Urlinger, S.2    Lohning, C.3    Prassler, J.4    Stark, Y.5    Jager, U.6    Hubner, B.7    Bardroff, M.8    Pradel, I.9    Boss, M.10
  • 46
    • 0036385795 scopus 로고    scopus 로고
    • Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy
    • Rubin S.M., Lee S.Y., Ruiz E.J., Pines A., and Wemmer D.E. Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy. J. Mol. Biol. 322 (2002) 425-440
    • (2002) J. Mol. Biol. , vol.322 , pp. 425-440
    • Rubin, S.M.1    Lee, S.Y.2    Ruiz, E.J.3    Pines, A.4    Wemmer, D.E.5
  • 47
    • 0032541623 scopus 로고    scopus 로고
    • Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a
    • Russo A.A., Tong L., Lee J.O., Jeffrey P.D., and Pavletich N.P. Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. Nature 395 (1998) 237-243
    • (1998) Nature , vol.395 , pp. 237-243
    • Russo, A.A.1    Tong, L.2    Lee, J.O.3    Jeffrey, P.D.4    Pavletich, N.P.5
  • 48
    • 0142242170 scopus 로고    scopus 로고
    • Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway
    • Schweizer A., Briand C., and Grütter M.G. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J. Biol. Chem. 278 (2003) 42441-42447
    • (2003) J. Biol. Chem. , vol.278 , pp. 42441-42447
    • Schweizer, A.1    Briand, C.2    Grütter, M.G.3
  • 50
    • 0032792551 scopus 로고    scopus 로고
    • The ankyrin repeat: a diversity of interactions on a common structural framework
    • Sedgwick S.G., and Smerdon S.J. The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 24 (1999) 311-316
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 311-316
    • Sedgwick, S.G.1    Smerdon, S.J.2
  • 51
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K., and Pos K.M. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313 (2006) 1295-1298
    • (2006) Science , vol.313 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Diederichs, K.5    Pos, K.M.6
  • 53
    • 0021818675 scopus 로고
    • Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface
    • Smith G.P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228 (1985) 1315-1317
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 56
    • 33644761961 scopus 로고    scopus 로고
    • Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA
    • Wilson J.J., and Kovall R.A. Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA. Cell 124 (2006) 985-996
    • (2006) Cell , vol.124 , pp. 985-996
    • Wilson, J.J.1    Kovall, R.A.2
  • 58
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution
    • Zhou Y., Morais-Cabral J.H., Kaufman A., and MacKinnon R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature 414 (2001) 43-48
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.