메뉴 건너뛰기




Volumn 334, Issue 4, 2003, Pages 721-731

Structure of an influenza neuraminidase-diabody complex by electron cryomicroscopy and image analysis

Author keywords

Diabody; Electron cryomicroscopy; Influenza neuraminidase; Recombinant antibody; Single particle reconstruction

Indexed keywords

PROTEIN; SIALIDASE;

EID: 0242636368     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.077     Document Type: Article
Times cited : (6)

References (41)
  • 1
    • 0035524114 scopus 로고    scopus 로고
    • Improving the efficacy of antibody-based cancer therapies
    • Carter P. Improving the efficacy of antibody-based cancer therapies. Nature Rev. Cancer. 1:2001;118-129.
    • (2001) Nature Rev. Cancer , vol.1 , pp. 118-129
    • Carter, P.1
  • 2
  • 3
    • 0004198722 scopus 로고
    • Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli
    • Huston J.S., Levinson D., Mudgett-Hunter M., Tai M.S., Novotny J., Margolies M.N., et al. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl Acad. Sci. USA. 85:1988;5879-5883.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 5879-5883
    • Huston, J.S.1    Levinson, D.2    Mudgett-Hunter, M.3    Tai, M.S.4    Novotny, J.5    Margolies, M.N.6
  • 5
    • 0027197493 scopus 로고
    • Diabodies: Small bivalent and bispecific antibody fragments
    • Holliger P., Prospero T., Winter G. Diabodies: small bivalent and bispecific antibody fragments. Proc. Natl Acad. Sci. USA. 90:1993;6444-6448.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6444-6448
    • Holliger, P.1    Prospero, T.2    Winter, G.3
  • 6
    • 0030748513 scopus 로고    scopus 로고
    • Triabodies: Single chain Fv fragments without a linker form trivalent trimers
    • Iliades P., Kortt A.A., Hudson P.J. Triabodies: single chain Fv fragments without a linker form trivalent trimers. FEBS Letters. 409:1997;437-441.
    • (1997) FEBS Letters , vol.409 , pp. 437-441
    • Iliades, P.1    Kortt, A.A.2    Hudson, P.J.3
  • 8
    • 0034906665 scopus 로고    scopus 로고
    • Biodistribution properties of (111)indium-labeled C-functionalized trans-cyclohexyl diethylenetriaminepentaacetic acid humanized 3S193 diabody and F(ab′)(2) constructs in a breast carcinoma xenograft model
    • Tahtis K., Lee F.T., Smyth F.E., Power B.E., Renner C., Brechbiel M.W., et al. Biodistribution properties of (111)indium-labeled C-functionalized trans-cyclohexyl diethylenetriaminepentaacetic acid humanized 3S193 diabody and F(ab′)(2) constructs in a breast carcinoma xenograft model. Clin. Cancer Res. 7:2001;1061-1072.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1061-1072
    • Tahtis, K.1    Lee, F.T.2    Smyth, F.E.3    Power, B.E.4    Renner, C.5    Brechbiel, M.W.6
  • 9
    • 0035077938 scopus 로고    scopus 로고
    • Tumor targeting of radiometal labeled anti-CEA recombinant T84.66 diabody and t84.66 minibody: Comparison to radioiodinated fragments
    • Yazaki P.J., Wu A.M., Tsai S.W., Williams L.E., Ikler D.N., Wong J.Y., et al. Tumor targeting of radiometal labeled anti-CEA recombinant T84.66 diabody and t84.66 minibody: comparison to radioiodinated fragments. Bioconjug. Chem. 12:2001;220-228.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 220-228
    • Yazaki, P.J.1    Wu, A.M.2    Tsai, S.W.3    Williams, L.E.4    Ikler, D.N.5    Wong, J.Y.6
  • 10
    • 0029932582 scopus 로고    scopus 로고
    • Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody
    • Holliger P., Brissinck J., Williams R.L., Thielemans K., Winter G. Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody. Protein Eng. 9:1996;299-305.
    • (1996) Protein Eng. , vol.9 , pp. 299-305
    • Holliger, P.1    Brissinck, J.2    Williams, R.L.3    Thielemans, K.4    Winter, G.5
  • 13
    • 0034603350 scopus 로고    scopus 로고
    • Influenza virus neuraminidase inhibitors
    • Gubareva L.V., Kaiser L., Hayden F.G. Influenza virus neuraminidase inhibitors. Lancet. 355:2000;827-835.
    • (2000) Lancet , vol.355 , pp. 827-835
    • Gubareva, L.V.1    Kaiser, L.2    Hayden, F.G.3
  • 14
    • 0029003145 scopus 로고
    • Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase
    • Varghese J.N., Epa V.C., Colman P.M. Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci. 4:1995;1081-1087.
    • (1995) Protein Sci. , vol.4 , pp. 1081-1087
    • Varghese, J.N.1    Epa, V.C.2    Colman, P.M.3
  • 15
    • 0032546756 scopus 로고    scopus 로고
    • Three-dimensional structures of single-chain Fv-neuraminidase complexes
    • Malby R.L., McCoy A.J., Kortt A.A., Hudson P.J., Colman P.M. Three-dimensional structures of single-chain Fv-neuraminidase complexes. J. Mol. Biol. 279:1998;901-910.
    • (1998) J. Mol. Biol. , vol.279 , pp. 901-910
    • Malby, R.L.1    Mccoy, A.J.2    Kortt, A.A.3    Hudson, P.J.4    Colman, P.M.5
  • 16
    • 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., et al. 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
  • 18
    • 0030953197 scopus 로고    scopus 로고
    • Single-chain Fv fragments of anti-neuraminidase antibody NC10 containing five- and ten-residue linkers form dimers and with zero-residue linker a trimer
    • Kortt A.A., Lah M., Oddie G.W., Gruen C.L., Burns J.E., Pearce L.A., et al. Single-chain Fv fragments of anti-neuraminidase antibody NC10 containing five- and ten-residue linkers form dimers and with zero-residue linker a trimer. Protein Eng. 10:1997;423-433.
    • (1997) Protein Eng. , vol.10 , pp. 423-433
    • Kortt, A.A.1    Lah, M.2    Oddie, G.W.3    Gruen, C.L.4    Burns, J.E.5    Pearce, L.A.6
  • 19
    • 0034830739 scopus 로고    scopus 로고
    • Dimeric and trimeric antibodies: High avidity scFvs for cancer targeting
    • Kortt A.A., Dolezal O., Power B.E., Hudson P.J. Dimeric and trimeric antibodies: high avidity scFvs for cancer targeting. Biomol. Eng. 18:2001;95-108.
    • (2001) Biomol. Eng. , vol.18 , pp. 95-108
    • Kortt, A.A.1    Dolezal, O.2    Power, B.E.3    Hudson, P.J.4
  • 20
    • 0032478777 scopus 로고    scopus 로고
    • Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments
    • Lawrence L.J., Kortt A.A., Iliades P., Tulloch P.A., Hudson P.J. Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments. FEBS Letters. 425:1998;479-484.
    • (1998) FEBS Letters , vol.425 , pp. 479-484
    • Lawrence, L.J.1    Kortt, A.A.2    Iliades, P.3    Tulloch, P.A.4    Hudson, P.J.5
  • 22
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
    • van Heel M. Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction. Ultramicroscopy. 21:1987;111-124.
    • (1987) Ultramicroscopy , vol.21 , pp. 111-124
    • Van Heel, M.1
  • 24
    • 0028774037 scopus 로고
    • The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody
    • Malby R.L., Tulip W.R., Harley V.R., McKimm-Breschkin J.L., Laver W.G., Webster R.G., Colman P.M. The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody. Structure. 2:1994;733-746.
    • (1994) Structure , vol.2 , pp. 733-746
    • Malby, R.L.1    Tulip, W.R.2    Harley, V.R.3    Mckimm-Breschkin, J.L.4    Laver, W.G.5    Webster, R.G.6    Colman, P.M.7
  • 25
    • 0001593953 scopus 로고
    • A packing function for delimiting the allowable locations of crystallized macromolecules
    • Hendrickson W.A., Ward K.B. A packing function for delimiting the allowable locations of crystallized macromolecules. Acta Crystallog. sect. A. 32:1976;778.
    • (1976) Acta Crystallog. sect. A , vol.32 , pp. 778
    • Hendrickson, W.A.1    Ward, K.B.2
  • 27
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice
    • Grigorieff N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice. J. Mol. Biol. 277:1998;1033-1046.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 28
    • 0022605670 scopus 로고
    • A new 3-D reconstruction scheme applied to the 50 S ribosomal subunit of E. coli
    • Radermacher M., Wagenknecht T., Verschoor A., Frank J. A new 3-D reconstruction scheme applied to the 50 S ribosomal subunit of E. coli. J. Microsc. 141:1986;RP1-RP2.
    • (1986) J. Microsc. , vol.141
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 29
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature. 386:1997;88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 30
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson R. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Quart. Rev. Biophys. 28:1995;171-193.
    • (1995) Quart. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 31
    • 0023710629 scopus 로고
    • Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint
    • Lesk A.M., Chothia C. Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint. Nature. 335:1988;188-190.
    • (1988) Nature , vol.335 , pp. 188-190
    • Lesk, A.M.1    Chothia, C.2
  • 33
    • 0037751777 scopus 로고
    • Holey films for electron microscopy
    • Harris J.W. Holey films for electron microscopy. Nature. 196:1962;499-500.
    • (1962) Nature , vol.196 , pp. 499-500
    • Harris, J.W.1
  • 34
    • 0023889015 scopus 로고
    • Containment system for the preparation of vitrified-hydrated virus specimens
    • Jeng T.W., Talmon Y., Chiu W. Containment system for the preparation of vitrified-hydrated virus specimens. J. Electron Microsc. Tech. 8:1988;343-348.
    • (1988) J. Electron Microsc. Tech. , vol.8 , pp. 343-348
    • Jeng, T.W.1    Talmon, Y.2    Chiu, W.3
  • 36
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:1996;190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 38
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 41
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • See also pp. 127-128
    • Evans S.V. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138. See also pp. 127-128.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.