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Volumn 45, Issue 25, 2006, Pages 7733-7739

Conformational features of the full-length HIV and SIV Nef proteins determined by mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; DATA REDUCTION; HYDROGEN; IMMUNOLOGY; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE; SIGNALING; VIRUSES; X RAY CRYSTALLOGRAPHY;

EID: 33746882478     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060438x     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 0034134113 scopus 로고    scopus 로고
    • Interactions of HIV-1 NEF with cellular signal transducing proteins
    • Renkema, G. H., and Saksela, K. (2000) Interactions of HIV-1 NEF with cellular signal transducing proteins, Front Biosci. 5, D268-D283.
    • (2000) Front Biosci. , vol.5
    • Renkema, G.H.1    Saksela, K.2
  • 2
    • 0034894379 scopus 로고    scopus 로고
    • Structure-function relationships in HIV-1 Nef
    • Geyer, M., Fackler, O. T., and Peterlin, B. M. (2001) Structure-function relationships in HIV-1 Nef, EMBO Rep. 2, 580-585.
    • (2001) EMBO Rep. , vol.2 , pp. 580-585
    • Geyer, M.1    Fackler, O.T.2    Peterlin, B.M.3
  • 3
    • 0035368515 scopus 로고    scopus 로고
    • Dynamic Nef and Nef dynamics: How structure could explain the complex activities of this small HIV protein
    • Arold, S. T., and Baur, A. S. (2001) Dynamic Nef and Nef dynamics: How structure could explain the complex activities of this small HIV protein, Trends Biochem. Sci. 26, 356-363.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 356-363
    • Arold, S.T.1    Baur, A.S.2
  • 4
    • 0036230879 scopus 로고    scopus 로고
    • Live and let die: Nef functions beyond HIV replication
    • Fackler, O. T., and Baur, A. S. (2002) Live and let die: Nef functions beyond HIV replication, Immunity 16, 493-497.
    • (2002) Immunity , vol.16 , pp. 493-497
    • Fackler, O.T.1    Baur, A.S.2
  • 5
    • 11444256754 scopus 로고    scopus 로고
    • Nef: "Necessary and enforcing factor" in HIV infection
    • Joseph, A. M., Kumar, M., and Mitra, D. (2005) Nef: "Necessary and enforcing factor" in HIV infection, Curr. HIV Res. 3, 87-94.
    • (2005) Curr. HIV Res. , vol.3 , pp. 87-94
    • Joseph, A.M.1    Kumar, M.2    Mitra, D.3
  • 7
    • 0032990431 scopus 로고    scopus 로고
    • Simian immunodeficiency virus and human immunodeficiency virus type 1 nef proteins show distinct patterns and mechanisms of Src kinase activation
    • Greenway, A. L., Dutartre, H., Allen, K., McPhee, D. A., Olive, D., and Collette, Y. (1999) Simian immunodeficiency virus and human immunodeficiency virus type 1 nef proteins show distinct patterns and mechanisms of Src kinase activation, J. Virol. 73, 6152-6158.
    • (1999) J. Virol. , vol.73 , pp. 6152-6158
    • Greenway, A.L.1    Dutartre, H.2    Allen, K.3    McPhee, D.A.4    Olive, D.5    Collette, Y.6
  • 8
    • 0034635475 scopus 로고    scopus 로고
    • HIV-2 and SIV nef proteins target different Src family SH3 domains than does HIV-1 Nef because of a triple amino acid substitution
    • Collette, Y., Arold, S., Picard, C., Janvier, K., Benichou, S., Benarous, R., Olive, D., and Dumas, C. (2000) HIV-2 and SIV nef proteins target different Src family SH3 domains than does HIV-1 Nef because of a triple amino acid substitution, J. Biol. Chem. 275, 4171-4176.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4171-4176
    • Collette, Y.1    Arold, S.2    Picard, C.3    Janvier, K.4    Benichou, S.5    Benarous, R.6    Olive, D.7    Dumas, C.8
  • 10
    • 0033995168 scopus 로고    scopus 로고
    • Simian immunodeficiency virus containing mutations in N-terminal tyrosine residues and in the PxxP motif in Nef replicates efficiently in rhesus macaques
    • Carl, S., Iafrate, A. J., Lang, S. M., Stolte, N., Stahl-Hennig, C., Matz-Rensing, K., Fuchs, D., Skowronski, J., and Kirchhoff, F. (2000) Simian immunodeficiency virus containing mutations in N-terminal tyrosine residues and in the PxxP motif in Nef replicates efficiently in rhesus macaques, J. Virol. 74, 4155-4164.
    • (2000) J. Virol. , vol.74 , pp. 4155-4164
    • Carl, S.1    Iafrate, A.J.2    Lang, S.M.3    Stolte, N.4    Stahl-Hennig, C.5    Matz-Rensing, K.6    Fuchs, D.7    Skowronski, J.8    Kirchhoff, F.9
  • 11
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • Grzesiek, S., Bax, A., Clore, G. M., Gronenborn, A. M., Hu, J. S., Kaufman, J., Palmer, I., Stahl, S. J., and Wingfield, P. T. (1996) The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase, Nat. Struct. Biol. 3, 340-345.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.S.5    Kaufman, J.6    Palmer, I.7    Stahl, S.J.8    Wingfield, P.T.9
  • 13
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee, C. H., Saksela, K., Mirza, U. A., Chait, B. T., and Kuriyan, J. (1996) Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain, Cell 85, 931-942.
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 14
    • 0031572847 scopus 로고    scopus 로고
    • The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling
    • Arold, S., Franken, P., Strub, M. P., Hoh, F., Benichou, S., Benarous, R., and Dumas, C. (1997) The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling, Structure 5, 1361-1372.
    • (1997) Structure , vol.5 , pp. 1361-1372
    • Arold, S.1    Franken, P.2    Strub, M.P.3    Hoh, F.4    Benichou, S.5    Benarous, R.6    Dumas, C.7
  • 15
    • 0033612388 scopus 로고    scopus 로고
    • Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein
    • Geyer, M., Munte, C. E., Schorr, J., Kellner, R., and Kalbitzer, H. R. (1999) Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein, J. Mol. Biol. 289, 123-138.
    • (1999) J. Mol. Biol. , vol.289 , pp. 123-138
    • Geyer, M.1    Munte, C.E.2    Schorr, J.3    Kellner, R.4    Kalbitzer, H.R.5
  • 16
    • 0030997633 scopus 로고    scopus 로고
    • Solution structure of a polypeptide from the N terminus of the HIV protein Nef
    • Barnham, K. J., Monks, S. A., Hinds, M. G., Azad, A. A., and Norton, R. S. (1997) Solution structure of a polypeptide from the N terminus of the HIV protein Nef, Biochemistry 36, 5970-5980.
    • (1997) Biochemistry , vol.36 , pp. 5970-5980
    • Barnham, K.J.1    Monks, S.A.2    Hinds, M.G.3    Azad, A.A.4    Norton, R.S.5
  • 17
    • 33144469859 scopus 로고    scopus 로고
    • Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef
    • Breuer, S., Gerlach, H., Kolaric, B., Urbanke, C., Opitz, N., and Geyer, M. (2006) Biochemical Indication for Myristoylation-Dependent Conformational Changes in HIV-1 Nef, Biochemistry 45, 2339-2349.
    • (2006) Biochemistry , vol.45 , pp. 2339-2349
    • Breuer, S.1    Gerlach, H.2    Kolaric, B.3    Urbanke, C.4    Opitz, N.5    Geyer, M.6
  • 18
    • 0035844009 scopus 로고    scopus 로고
    • Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef
    • Geyer, M., and Peterlin, B. M. (2001) Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef, FEBS Lett. 496, 91-95.
    • (2001) FEBS Lett. , vol.496 , pp. 91-95
    • Geyer, M.1    Peterlin, B.M.2
  • 19
    • 0033013962 scopus 로고    scopus 로고
    • Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-Terminal α helix and proline repeat of Nef selectively regulate MHC-I trafficking
    • Mangasarian, A., Piguet, V., Wang, J. K., Chen, Y. L., and Trono, D. (1999) Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-Terminal α helix and proline repeat of Nef selectively regulate MHC-I trafficking, J. Virol. 73, 1964-1973.
    • (1999) J. Virol. , vol.73 , pp. 1964-1973
    • Mangasarian, A.1    Piguet, V.2    Wang, J.K.3    Chen, Y.L.4    Trono, D.5
  • 20
    • 0034001233 scopus 로고    scopus 로고
    • Nef-induced major histocompatibility complex class I down-regulation is functionally dissociated from its virion incorporation, enhancement of viral infectivity, and CD4 down-regulation
    • Akari, H., Arold, S., Fukumori, T., Okazaki, T., Strebel, K., and Adachi, A. (2000) Nef-induced major histocompatibility complex class I down-regulation is functionally dissociated from its virion incorporation, enhancement of viral infectivity, and CD4 down-regulation, J. Virol. 74, 2907-2912.
    • (2000) J. Virol. , vol.74 , pp. 2907-2912
    • Akari, H.1    Arold, S.2    Fukumori, T.3    Okazaki, T.4    Strebel, K.5    Adachi, A.6
  • 21
    • 0032525137 scopus 로고    scopus 로고
    • The SH3 domain-binding surface and an acidic motif in HIV-1 Nef regulate trafficking of class I MHC complexes
    • Greenberg, M. E., Iafrate, A. J., and Skowronski, J. (1998) The SH3 domain-binding surface and an acidic motif in HIV-1 Nef regulate trafficking of class I MHC complexes, EMBO J. 17, 2777-2789.
    • (1998) EMBO J. , vol.17 , pp. 2777-2789
    • Greenberg, M.E.1    Iafrate, A.J.2    Skowronski, J.3
  • 22
    • 0029924038 scopus 로고    scopus 로고
    • Mutational analysis of HIV-1 Nef: Identification of two mutants that are temperature-sensitive for CD4 downregulation
    • Aiken, C., Krause, L., Chen, Y. L., and Trono, D. (1996) Mutational analysis of HIV-1 Nef: Identification of two mutants that are temperature-sensitive for CD4 downregulation, Virology 217, 293-300.
    • (1996) Virology , vol.217 , pp. 293-300
    • Aiken, C.1    Krause, L.2    Chen, Y.L.3    Trono, D.4
  • 23
    • 24644466459 scopus 로고    scopus 로고
    • Co-translational myristoylation alters the quaternary structure of HIV-1 Nef in solution
    • Dennis, C. A., Baron, A., Grossmann, J. G., Mazaleyrat, S., Harris, M., and Jaeger, J. (2005) Co-translational myristoylation alters the quaternary structure of HIV-1 Nef in solution, Proteins 60, 658-669.
    • (2005) Proteins , vol.60 , pp. 658-669
    • Dennis, C.A.1    Baron, A.2    Grossmann, J.G.3    Mazaleyrat, S.4    Harris, M.5    Jaeger, J.6
  • 24
    • 0030016181 scopus 로고    scopus 로고
    • Autophosphorylation of the Fes tyrosine kinase. Evidence for an intermolecular mechanism involving two kinase domain tyrosine residues
    • Rogers, J. A., Read, R. D., Li, J., Peters, K. L., and Smithgall, T. E. (1996) Autophosphorylation of the Fes tyrosine kinase. Evidence for an intermolecular mechanism involving two kinase domain tyrosine residues, J. Biol. Chem. 271, 17519-17525.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17519-17525
    • Rogers, J.A.1    Read, R.D.2    Li, J.3    Peters, K.L.4    Smithgall, T.E.5
  • 25
    • 0038121525 scopus 로고    scopus 로고
    • Analysis of protein complexes with hydrogen exchange and mass spectrometry
    • Engen, J. R. (2003) Analysis of protein complexes with hydrogen exchange and mass spectrometry, Analyst 128, 3-8.
    • (2003) Analyst , vol.128 , pp. 3-8
    • Engen, J.R.1
  • 26
    • 0033655078 scopus 로고    scopus 로고
    • Investigating the higher order structure of proteins. Hydrogen exchange, proteolytic fragmentation, and mass spectrometry
    • Engen, J. R., and Smith, D. L. (2000) Investigating the higher order structure of proteins. Hydrogen exchange, proteolytic fragmentation, and mass spectrometry, Methods Mol. Biol. 146, 95-112.
    • (2000) Methods Mol. Biol. , vol.146 , pp. 95-112
    • Engen, J.R.1    Smith, D.L.2
  • 27
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang, Z., and Smith, D. L. (1993) Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation, Protein Sci. 2, 522-531.
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 28
    • 1842863972 scopus 로고    scopus 로고
    • Practical methods for deuterium exchange/mass spectrometry
    • Hoofnagle, A. N., Resing, K. A., and Ahn, N. G. (2004) Practical methods for deuterium exchange/mass spectrometry, Methods Mol. Biol. 250, 283-298.
    • (2004) Methods Mol. Biol. , vol.250 , pp. 283-298
    • Hoofnagle, A.N.1    Resing, K.A.2    Ahn, N.G.3
  • 29
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: Optimization of digestion conditions
    • Wang, L., Pan, H., and Smith, D. L. (2002) Hydrogen exchange-mass spectrometry: Optimization of digestion conditions, Mol. Cell. Proteomics 1, 132-138.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 30
    • 0025398721 scopus 로고
    • What if: A molecular modeling and drug design program
    • Vriend, G. (1990) WHAT IF: A molecular modeling and drug design program, J. Mol. Graphics 8, 29, 52-56.
    • (1990) J. Mol. Graphics , vol.8 , pp. 29
    • Vriend, G.1
  • 31
    • 0001913048 scopus 로고    scopus 로고
    • Predicting protein disorder for N-, C-, and internal regions
    • Li, X., Romero, P., Rani, M., Dunker, A. K., and Obradovic, Z. (1999) Predicting protein disorder for N-, C-, and internal regions, Genome Inf. 10, 30-40.
    • (1999) Genome Inf. , vol.10 , pp. 30-40
    • Li, X.1    Romero, P.2    Rani, M.3    Dunker, A.K.4    Obradovic, Z.5
  • 32
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith, D. L., Deng, Y., and Zhang, Z. (1997) Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry, J. Mass Spectrom. 32, 135-146.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 34
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales, T. E., and Engen, J. R. (2006) Hydrogen exchange mass spectrometry for the analysis of protein dynamics, Mass Spectrom. Rev. 25, 158-170.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 35
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S. W., and Kallenbach, N. R. (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids, Q. Rev. Biophys. 16, 521-655.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2


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