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Volumn 366, Issue 5, 2007, Pages 1538-1544

The Coiled-coil Domain Structure of the Sin Nombre Virus Nucleocapsid Protein

Author keywords

antiparallel coiled coil; crystal structure; hantavirus; mini fibritin; Sin Nombre virus

Indexed keywords

GENOMIC RNA; NUCLEOCAPSID PROTEIN; RIBONUCLEOPROTEIN;

EID: 33846828595     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.12.046     Document Type: Article
Times cited : (30)

References (24)
  • 1
    • 0031113395 scopus 로고    scopus 로고
    • Hantaviruses: a global disease problem
    • Schmaljohn C., and Hjelle B. Hantaviruses: a global disease problem. Emerg. Infect. Dis. 3 (1997) 95-104
    • (1997) Emerg. Infect. Dis. , vol.3 , pp. 95-104
    • Schmaljohn, C.1    Hjelle, B.2
  • 2
    • 33846849910 scopus 로고    scopus 로고
    • Elliott, R.M., Bouloy, M., Calisher, C.H., Goldbach, R., Moyer, J.T., Nichol, S.T., et al. (2000). Family Bunyaviridae. In Virus Taxonomy (van Regenmortel, M.H.V., Fauquet, C.M., Bishop, D.H.L., Carsten, E.B., Estes, M.K. & Lemon, S.M. et al., eds), pp. 599-621, Academic Press, San Diego.
  • 3
    • 23844454526 scopus 로고    scopus 로고
    • Hantavirus nucleocapsid protein: a multifunctional molecule with both housekeeping and ambassadorial duties
    • Kaukinen P., Vaheri A., and Plyusnin A. Hantavirus nucleocapsid protein: a multifunctional molecule with both housekeeping and ambassadorial duties. Arch. Virol. 150 (2005) 1693-1713
    • (2005) Arch. Virol. , vol.150 , pp. 1693-1713
    • Kaukinen, P.1    Vaheri, A.2    Plyusnin, A.3
  • 7
    • 3242713982 scopus 로고    scopus 로고
    • Trimeric hantavirus nucleocapsid protein binds specifically to the viral RNA panhandle
    • Mir M.A., and Panganiban A.T. Trimeric hantavirus nucleocapsid protein binds specifically to the viral RNA panhandle. J. Virol. 78 (2004) 8281-8288
    • (2004) J. Virol. , vol.78 , pp. 8281-8288
    • Mir, M.A.1    Panganiban, A.T.2
  • 8
    • 22544442477 scopus 로고    scopus 로고
    • Essential amino acids of the Hantaan virus N protein in its interaction with RNA
    • Severson W., Xu X., Kuhn M., Senutovitch N., Thokala M., Ferron F., et al. Essential amino acids of the Hantaan virus N protein in its interaction with RNA. J. Virol. 79 (2005) 10032-10039
    • (2005) J. Virol. , vol.79 , pp. 10032-10039
    • Severson, W.1    Xu, X.2    Kuhn, M.3    Senutovitch, N.4    Thokala, M.5    Ferron, F.6
  • 9
    • 0036122461 scopus 로고    scopus 로고
    • The RNA binding domain of the Hantaan virus N protein maps to a central, conserved region
    • Xu X., Severson W., Villegas N., Schmaljohn C.S., and Jonsson C.B. The RNA binding domain of the Hantaan virus N protein maps to a central, conserved region. J. Virol. 76 (2002) 3301-3308
    • (2002) J. Virol. , vol.76 , pp. 3301-3308
    • Xu, X.1    Severson, W.2    Villegas, N.3    Schmaljohn, C.S.4    Jonsson, C.B.5
  • 10
    • 0141454820 scopus 로고    scopus 로고
    • Mapping of the regions involved in homotypic interactions of Tula hantavirus N protein
    • Kaukinen P., Vaheri A., and Plyusnin A. Mapping of the regions involved in homotypic interactions of Tula hantavirus N protein. J. Virol. 77 (2003) 10910-10916
    • (2003) J. Virol. , vol.77 , pp. 10910-10916
    • Kaukinen, P.1    Vaheri, A.2    Plyusnin, A.3
  • 11
    • 0037225705 scopus 로고    scopus 로고
    • The multimerization of hantavirus nucleocapsid protein depends on type-specific epitopes
    • Yoshimatsu K., Lee B.H., Araki K., Morimatsu M., Ogino M., Ebihara H., et al. The multimerization of hantavirus nucleocapsid protein depends on type-specific epitopes. J. Virol. 77 (2003) 943-952
    • (2003) J. Virol. , vol.77 , pp. 943-952
    • Yoshimatsu, K.1    Lee, B.H.2    Araki, K.3    Morimatsu, M.4    Ogino, M.5    Ebihara, H.6
  • 12
    • 10044281964 scopus 로고    scopus 로고
    • Oligomerization of hantavirus N protein: C-terminal α-helices interact to form a shared hydrophobic space
    • Kaukinen P., Kumar V., Tulimäki K., Engelhardt P., Vaheri A., and Plyusnin A. Oligomerization of hantavirus N protein: C-terminal α-helices interact to form a shared hydrophobic space. J. Virol. 78 (2004) 13669-13677
    • (2004) J. Virol. , vol.78 , pp. 13669-13677
    • Kaukinen, P.1    Kumar, V.2    Tulimäki, K.3    Engelhardt, P.4    Vaheri, A.5    Plyusnin, A.6
  • 13
    • 33748479919 scopus 로고    scopus 로고
    • Oligomerization of hantavirus nucleocapsid protein: analysis of the N-terminal coiled-coil domain
    • Alminaite A., Halttunen V., Kumar V., Vaheri A., Holm L., and Plyusnin A. Oligomerization of hantavirus nucleocapsid protein: analysis of the N-terminal coiled-coil domain. J. Virol. 80 (2006) 9073-9081
    • (2006) J. Virol. , vol.80 , pp. 9073-9081
    • Alminaite, A.1    Halttunen, V.2    Kumar, V.3    Vaheri, A.4    Holm, L.5    Plyusnin, A.6
  • 14
    • 25444502378 scopus 로고    scopus 로고
    • Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier
    • Bachmann A., Kiefhaber T., Boudko S., Engel J., and Bachinger H.P. Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier. Proc. Natl Acad. Sci. USA 102 (2005) 13897-13902
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13897-13902
    • Bachmann, A.1    Kiefhaber, T.2    Boudko, S.3    Engel, J.4    Bachinger, H.P.5
  • 15
    • 0346022969 scopus 로고    scopus 로고
    • Structure formation in the C terminus of type III collagen guides disulfide cross-linking
    • Boudko S.P., and Engel J. Structure formation in the C terminus of type III collagen guides disulfide cross-linking. J. Mol. Biol. 335 (2004) 1289-1297
    • (2004) J. Mol. Biol. , vol.335 , pp. 1289-1297
    • Boudko, S.P.1    Engel, J.2
  • 16
    • 2542468691 scopus 로고    scopus 로고
    • Design and crystal structure of bacteriophage T4 mini-fibritin NCCF
    • Boudko S.P., Strelkov S.V., Engel J., and Stetefeld J. Design and crystal structure of bacteriophage T4 mini-fibritin NCCF. J. Mol. Biol. 339 (2004) 927-935
    • (2004) J. Mol. Biol. , vol.339 , pp. 927-935
    • Boudko, S.P.1    Strelkov, S.V.2    Engel, J.3    Stetefeld, J.4
  • 17
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 18
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction measurements
    • Hendrickson W.A., and Ogata C.M. Phase determination from multiwavelength anomalous diffraction measurements. Methods Enzymol. 276 (1997) 494-523
    • (1997) Methods Enzymol. , vol.276 , pp. 494-523
    • Hendrickson, W.A.1    Ogata, C.M.2
  • 20
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger T.C. Automated structure solution, density modification and model building. Acta Crystallog. sect. D 58 (2002) 1937-1940
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 21
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit- a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit- a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 24
    • 84920325457 scopus 로고
    • AMoRe- an automated package for molecular replacement
    • Navaza J. AMoRe- an automated package for molecular replacement. Acta Crystallog. sect. A 50 (1994) 157-163
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 157-163
    • Navaza, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.