메뉴 건너뛰기




Volumn 79, Issue 22, 2005, Pages 14088-14094

Crystal structure of enteric adenovirus serotype 41 short fiber head

Author keywords

[No Author keywords available]

Indexed keywords

COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR; PEPSIN A; VIRUS FIBER PROTEIN;

EID: 27644511195     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.22.14088-14094.2005     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0032880731 scopus 로고    scopus 로고
    • Adenovirus type 41 lacks an RGD alpha(v)-integrin binding motif on the penton base and undergoes delayed uptake in A549 cells
    • Albinsson, B., and A. H. Kidd. 1999. Adenovirus type 41 lacks an RGD alpha(v)-integrin binding motif on the penton base and undergoes delayed uptake in A549 cells. Virus Res. 64:125-136.
    • (1999) Virus Res. , vol.64 , pp. 125-136
    • Albinsson, B.1    Kidd, A.H.2
  • 2
    • 0030017889 scopus 로고    scopus 로고
    • Analysis of topological and nontopological structural similarities in the PDB: New examples with old structures
    • Alexandrov, N. N., and D. Fischer. 1996. Analysis of topological and nontopological structural similarities in the PDB: new examples with old structures. Proteins 25:354-365.
    • (1996) Proteins , vol.25 , pp. 354-365
    • Alexandrov, N.N.1    Fischer, D.2
  • 3
    • 0027221062 scopus 로고
    • Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells
    • Bai, M., B. Harfe, and P. Freimuth. 1993. Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells. J. Virol. 67:5198-5205.
    • (1993) J. Virol. , vol.67 , pp. 5198-5205
    • Bai, M.1    Harfe, B.2    Freimuth, P.3
  • 5
    • 0033584785 scopus 로고    scopus 로고
    • Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR
    • Bewley, M. C., K. Springer, Y. B. Zhang, P. Freimuth, and J. M. Flanagan. 1999. Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR. Science 286:1579-1583.
    • (1999) Science , vol.286 , pp. 1579-1583
    • Bewley, M.C.1    Springer, K.2    Zhang, Y.B.3    Freimuth, P.4    Flanagan, J.M.5
  • 6
    • 3142729320 scopus 로고    scopus 로고
    • Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites
    • Burmeister, W. P., D. Guilligay, S. Cusack, G. Wadell, and N. Arnberg. 2004. Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. J. Virol. 78:7727-7736.
    • (2004) J. Virol. , vol.78 , pp. 7727-7736
    • Burmeister, W.P.1    Guilligay, D.2    Cusack, S.3    Wadell, G.4    Arnberg, N.5
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 9
    • 0031593872 scopus 로고    scopus 로고
    • In vitro and in vivo assessment of adenovirus 41 as a vector for gene delivery to the intestine
    • Croyle, M. A., M. Stone, G. L. Amidon, and B. J. Roessler. 1998. In vitro and in vivo assessment of adenovirus 41 as a vector for gene delivery to the intestine. Gene Ther. 5:645-654.
    • (1998) Gene Ther. , vol.5 , pp. 645-654
    • Croyle, M.A.1    Stone, M.2    Amidon, G.L.3    Roessler, B.J.4
  • 13
    • 0019440664 scopus 로고
    • Proteolytic enhancement of rotavirus infectivity: Molecular mechanisms
    • Estes, M. K., D. Y. Graham, and B. B. Mason. 1981. Proteolytic enhancement of rotavirus infectivity: molecular mechanisms. J. Virol. 39:879-888.
    • (1981) J. Virol. , vol.39 , pp. 879-888
    • Estes, M.K.1    Graham, D.Y.2    Mason, B.B.3
  • 14
    • 1942518221 scopus 로고    scopus 로고
    • Unique physico-chemical properties of human enteric Ad41 responsible for its survival and replication in the gastrointestinal tract
    • Favier, A. L., W. P. Burmeister, and J. Chroboczek. 2004. Unique physico-chemical properties of human enteric Ad41 responsible for its survival and replication in the gastrointestinal tract. Virology 322:93-104.
    • (2004) Virology , vol.322 , pp. 93-104
    • Favier, A.L.1    Burmeister, W.P.2    Chroboczek, J.3
  • 16
    • 0029934092 scopus 로고    scopus 로고
    • A human cell line selected for resistance to adenovirus infection has reduced levels of the virus receptor
    • Freimuth, P. 1996. A human cell line selected for resistance to adenovirus infection has reduced levels of the virus receptor. J. Virol. 70:4081-4085.
    • (1996) J. Virol. , vol.70 , pp. 4081-4085
    • Freimuth, P.1
  • 17
    • 0345708273 scopus 로고    scopus 로고
    • CD46 is a cellular receptor for group B adenoviruses
    • Gaggar, A., D. M. Shayakhmetov, and A. Lieber. 19 October 2003. CD46 is a cellular receptor for group B adenoviruses. Nat. Med. 9:1408-1412.
    • (2003) Nat. Med. , vol.9 , pp. 1408-1412
    • Gaggar, A.1    Shayakhmetov, D.M.2    Lieber, A.3
  • 18
    • 0030464460 scopus 로고    scopus 로고
    • SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny
    • Galtier, N., M. Gouy, and C. Gautier. 1996. SEAVIEW and PHYLO_WIN: two graphic tools for sequence alignment and molecular phylogeny. Comput. Appl. Biosci. 12:543-548.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2    Gautier, C.3
  • 19
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., E. Courcelle, D. I. Stuart, and F. Metoz. 1999. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 20
    • 0037492806 scopus 로고    scopus 로고
    • Structural basis for variation in adenovirus affinity for the cellular coxsackievirus and adenovirus receptor
    • Howitt, J., M. C. Bewley, V. Graziano, J. M. Flanagan, and P. Freimuth. 2003. Structural basis for variation in adenovirus affinity for the cellular coxsackievirus and adenovirus receptor. J. Biol. Chem. 278:26208-26215.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26208-26215
    • Howitt, J.1    Bewley, M.C.2    Graziano, V.3    Flanagan, J.M.4    Freimuth, P.5
  • 21
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. 1988. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21:916-924.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 22
    • 0027186306 scopus 로고
    • Adenovirus type 40 virions contain two distinct fibers
    • Kidd, A. H., J. Chroboczek, S. Cusack, and R. W. Ruigrok. 1993. Adenovirus type 40 virions contain two distinct fibers. Virology 192:73-84.
    • (1993) Virology , vol.192 , pp. 73-84
    • Kidd, A.H.1    Chroboczek, J.2    Cusack, S.3    Ruigrok, R.W.4
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 24
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsl
    • Leslie, A. G. W. 1992. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsl. Protein Crystallogr. 26.
    • (1992) Protein Crystallogr. , pp. 26
    • Leslie, A.G.W.1
  • 25
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. 1999. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 27
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., K. A. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 28
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., R. Morris, and V. S. Lamzin. 1999. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol 6:458-463.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 29
    • 0031666742 scopus 로고    scopus 로고
    • The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F
    • Roelvink, P. W., A. Lizonova, J. G. Lee, Y. Li, J. M. Bergelson, R. W. Finberg, D. E. Brough, I. Kovesdi, and T. J. Wickham. 1998. The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F. J. Virol. 72:7909-7915.
    • (1998) J. Virol. , vol.72 , pp. 7909-7915
    • Roelvink, P.W.1    Lizonova, A.2    Lee, J.G.3    Li, Y.4    Bergelson, J.M.5    Finberg, R.W.6    Brough, D.E.7    Kovesdi, I.8    Wickham, T.J.9
  • 32
    • 0030915715 scopus 로고    scopus 로고
    • HCAR and MCAR: The human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
    • Tomko, R. P., R. Xu, and L. Philipson. 1997. HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc. Natl. Acad. Sci. USA 94:3352-3356.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3352-3356
    • Tomko, R.P.1    Xu, R.2    Philipson, L.3
  • 33
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin, A., and A. Teplyakov. 2000. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56:1622-1624.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 34
    • 0033619203 scopus 로고    scopus 로고
    • Structure of the human adenovirus serotype 2 fiber head domain at 1.5 a resolution
    • van Raaij, M. J., N. Louis, J. Chroboczek, and S. Cusack. 1999. Structure of the human adenovirus serotype 2 fiber head domain at 1.5 A resolution. Virology 262:333-343.
    • (1999) Virology , vol.262 , pp. 333-343
    • Raaij, M.J.1    Louis, N.2    Chroboczek, J.3    Cusack, S.4
  • 35
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., R. A. Laskowski, and J. M. Thornton. 1995. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8:127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 36
    • 0037145045 scopus 로고    scopus 로고
    • Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape
    • Walters, R. W., P. Freimuth, T. O. Moninger, I. Ganske, J. Zabner, and M. J. Welsh. 2002. Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape. Cell 110:789-799.
    • (2002) Cell , vol.110 , pp. 789-799
    • Walters, R.W.1    Freimuth, P.2    Moninger, T.O.3    Ganske, I.4    Zabner, J.5    Welsh, M.J.6
  • 37
    • 0027166647 scopus 로고
    • Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment
    • Wickham, T. J., P. Mathias, D. A. Cheresh, and G. R. Nemerow. 1993. Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment. Cell 73:309-319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 38
    • 1842432490 scopus 로고    scopus 로고
    • Membrane cofactor protein is a receptor for adenoviruses associated with epidemic keratoconjunctivitis
    • Wu, E., S. A. Trauger, L. Pache, T. M. Mullen, D. J. von Seggern, G. Siuzdak, and G. R. Nemerow. 2004. Membrane cofactor protein is a receptor for adenoviruses associated with epidemic keratoconjunctivitis. J. Virol. 78:3897-3905.
    • (2004) J. Virol. , vol.78 , pp. 3897-3905
    • Wu, E.1    Trauger, S.A.2    Pache, L.3    Mullen, T.M.4    Von Seggern, D.J.5    Siuzdak, G.6    Nemerow, G.R.7
  • 39
    • 0028774724 scopus 로고
    • Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 a resolution
    • Xia, D., L. J. Henry, R. D. Gerard, and J. Deisenhofer. 1994. Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution. Structure 2:1259-1270.
    • (1994) Structure , vol.2 , pp. 1259-1270
    • Xia, D.1    Henry, L.J.2    Gerard, R.D.3    Deisenhofer, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.