메뉴 건너뛰기




Volumn 290, Issue 5, 1999, Pages 1031-1041

LearnCoil-VMF: Computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins

Author keywords

Coiled coil; Computational methods; Filovirus; Paramyxovirus; Retrovirus; Viral membrane fusion

Indexed keywords

VIRUS PROTEIN;

EID: 0033618320     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2796     Document Type: Article
Times cited : (138)

References (61)
  • 2
    • 0027480350 scopus 로고
    • Design of a discriminating fingerprint for G-protein-coupled receptors
    • Attwood T. K., Findlay J. B. C. Design of a discriminating fingerprint for G-protein-coupled receptors. Protein Eng. 6:1993;167-176.
    • (1993) Protein Eng. , vol.6 , pp. 167-176
    • Attwood, T.K.1    Findlay, J.B.C.2
  • 4
    • 0029258846 scopus 로고
    • Algorithms for protein structural motif recognition
    • Berger B. Algorithms for protein structural motif recognition. J. Comput. Biol. 2:1995;125-138.
    • (1995) J. Comput. Biol. , vol.2 , pp. 125-138
    • Berger, B.1
  • 5
    • 0030831197 scopus 로고    scopus 로고
    • An iterative method for improved protein structural motif recognition
    • Berger B., Singh M. An iterative method for improved protein structural motif recognition. J. Comput. Biol. 4:1997;261-273.
    • (1997) J. Comput. Biol. , vol.4 , pp. 261-273
    • Berger, B.1    Singh, M.2
  • 7
    • 0024974115 scopus 로고
    • Too many leucine zippers?
    • Brendel V., Karlin S. Too many leucine zippers? Nature. 341:1989;574-575.
    • (1989) Nature , vol.341 , pp. 574-575
    • Brendel, V.1    Karlin, S.2
  • 8
    • 0028023726 scopus 로고
    • Structure of influenza hemagglutinin at the pH of membrane fusion
    • Bullough P. A., Hughson F. M., Skehel J. J., Wiley D. C. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature. 371:1994;37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 10
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr C., Kim P. S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:1993;823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.1    Kim, P.S.2
  • 11
    • 0025678671 scopus 로고
    • Heptad repeat regions are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers P., Pringle C., Easton A. Heptad repeat regions are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71:1990;3075-3080.
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.2    Easton, A.3
  • 12
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D., Kim P. S. HIV entry and its inhibition. Cell. 93:1998;681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.1    Kim, P.S.2
  • 13
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D., Fass D., Berger J. M., Kim P. S. Core structure of gp41 from the HIV envelope glycoprotein. Cell. 89:1997;263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 14
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV-1 gp41 is an attractive drug target
    • Chan D., Chutkowski C., Kim P. S. Evidence that a prominent cavity in the coiled coil of HIV-1 gp41 is an attractive drug target. Proc. Natl Acad. Sci. USA. 95:1998;15613-15617.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.1    Chutkowski, C.2    Kim, P.S.3
  • 15
    • 0027973132 scopus 로고
    • SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils
    • Chapman E., An S., Barton N., Jahn R. SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils. J. Biol. Chem. 269:1994;27427-27432.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27427-27432
    • Chapman, E.1    An, S.2    Barton, N.3    Jahn, R.4
  • 16
    • 0029072191 scopus 로고
    • A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: Implication for viral fusion
    • Chen C., Matthews T., McDanal C., Bolognesi D., Greenberg M. A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J. Virol. 69:1995;3771-3777.
    • (1995) J. Virol. , vol.69 , pp. 3771-3777
    • Chen, C.1    Matthews, T.2    McDanal, C.3    Bolognesi, D.4    Greenberg, M.5
  • 17
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a leucine zipper-like repeat
    • Delwart E., Moialos G., Gilmore T. Retroviral envelope glycoproteins contain a leucine zipper-like repeat. AIDS Res. Hum. Retroviruses. 6:1990;703-706.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 703-706
    • Delwart, E.1    Moialos, G.2    Gilmore, T.3
  • 18
    • 0024999332 scopus 로고
    • Improved detection of helix-turn-helix DNA-binding motifs in protein sequences
    • Dodd I., Egan J. B. Improved detection of helix-turn-helix DNA-binding motifs in protein sequences. Nucl. Acids Res. 18:1990;5019-5026.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 5019-5026
    • Dodd, I.1    Egan, J.B.2
  • 19
    • 0029556891 scopus 로고
    • Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin
    • Fass D., Kim P. S. Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin. Curr. Biol. 5:1995;1377-1383.
    • (1995) Curr. Biol. , vol.5 , pp. 1377-1383
    • Fass, D.1    Kim, P.S.2
  • 20
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 Angstrom resolution
    • Fass D., Harrison S., Kim P. S. Retrovirus envelope domain at 1.7 Angstrom resolution. Nature Struct. Biol. 3:1996;465-469.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.2    Kim, P.S.3
  • 21
    • 0031041456 scopus 로고    scopus 로고
    • A structural change occurs upon binding of syntaxin to SNAP-25
    • Fasshauer D., Bruns D., Shen B., Jahn R., Brünger A. A structural change occurs upon binding of syntaxin to SNAP-25. J. Biol. Chem. 272:1997;4582-4590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4582-4590
    • Fasshauer, D.1    Bruns, D.2    Shen, B.3    Jahn, R.4    Brünger, A.5
  • 23
    • 0030591276 scopus 로고    scopus 로고
    • Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses
    • Gallaher W. Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses. Cell. 85:1996;477-478.
    • (1996) Cell , vol.85 , pp. 477-478
    • Gallaher, W.1
  • 25
    • 0026730491 scopus 로고
    • Translational initiation factors IF-1 and eIF-2α share an RNA-binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase
    • Gribskov M. Translational initiation factors IF-1 and eIF-2α share an RNA-binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase. Gene. 119:1992;107-111.
    • (1992) Gene , vol.119 , pp. 107-111
    • Gribskov, M.1
  • 27
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson P., Roth R., Morisaki H., Jahn R., Heuser J. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell. 90:1997;523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.5
  • 28
    • 0027756896 scopus 로고
    • A switch between two-, three- And four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P. B., Zhang T., Kim P. S., Alber T. A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 29
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi T., McMahon H., Yamasaki S., Binz T., Hata Y., Südhof T., Niemann H. Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13:1994;5051-5061.
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.6    Niemann, H.7
  • 30
    • 0031240001 scopus 로고    scopus 로고
    • Enveloped viruses: A common mode of membrane fusion?
    • Hughson F. Enveloped viruses: a common mode of membrane fusion? Curr. Biol. 7:1997;R565-R569.
    • (1997) Curr. Biol. , vol.7
    • Hughson, F.1
  • 31
    • 0026660586 scopus 로고
    • Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1
    • Inoue A., Obata K., Akagawa K. Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1. J. Biol. Chem. 267:1992;10613-10619.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10613-10619
    • Inoue, A.1    Obata, K.2    Akagawa, K.3
  • 32
    • 0027179560 scopus 로고
    • HIV-1 inhibition by a peptide
    • Jiang S., Lin K., Neurath A. HIV-1 inhibition by a peptide. Nature. 365:1993;113.
    • (1993) Nature , vol.365 , pp. 113
    • Jiang, S.1    Lin, K.2    Neurath, A.3
  • 33
    • 0032529672 scopus 로고    scopus 로고
    • A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41
    • Joshi S., Dutch R., Lamb R. A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology. 248:1998;20-34.
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.1    Dutch, R.2    Lamb, R.3
  • 36
    • 0027912333 scopus 로고
    • Detecting subtle sequence signals: A Gibbs sampling strategy for multiple alignment
    • Lawrence C., Altschul S., Boguski M., Liu J., Neuwald A., Wootton J. Detecting subtle sequence signals: a Gibbs sampling strategy for multiple alignment. Science. 262:1993;208-214.
    • (1993) Science , vol.262 , pp. 208-214
    • Lawrence, C.1    Altschul, S.2    Boguski, M.3    Liu, J.4    Neuwald, A.5    Wootton, J.6
  • 37
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin R., Scheller R. Structural organization of the synaptic exocytosis core complex. Neuron. 19:1997;1087-1094.
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.1    Scheller, R.2
  • 38
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M., Blacklow S., Kim P. S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct. Biol. 2:1995;1075-1082.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.2    Kim, P.S.3
  • 39
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., van Dyke M., Stock J. Predicting coiled coils from protein sequences. Science. 252:1991;1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 40
    • 0032483021 scopus 로고    scopus 로고
    • Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: Conserved helical interactions underlie the broad inhibitory activity of gp41 peptides
    • Malashkevich V. N., Chan D., Chutkowski C., Kim P. S. Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc. Natl Acad. Sci. USA. 95:1998;9134-9139.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9134-9139
    • Malashkevich, V.N.1    Chan, D.2    Chutkowski, C.3    Kim, P.S.4
  • 44
    • 0020446736 scopus 로고
    • Coiled coils in alpha-helix-containing proteins: Analysis of residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry D. A. D. Coiled coils in alpha-helix-containing proteins: analysis of residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci. Rep. 2:1982;1017-1024.
    • (1982) Biosci. Rep. , vol.2 , pp. 1017-1024
    • Parry, D.A.D.1
  • 45
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: An emerging similarity with functional domains of other viruses
    • Rapaport D., Ovadia M., Shai Y. A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: an emerging similarity with functional domains of other viruses. EMBO J. 14:1995;5524-5531.
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 46
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Angstrom resolution
    • Rey F., Heinz F., Mandl C., Kunz C., Harrison S. The envelope glycoprotein from tick-borne encephalitis virus at 2 Angstrom resolution. Nature. 375:1995;291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.1    Heinz, F.2    Mandl, C.3    Kunz, C.4    Harrison, S.5
  • 47
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70 % accuracy
    • Rost B., Sander C. Prediction of protein structure at better than 70 % accuracy. J. Mol. Biol. 232:1993;584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 48
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins: Struct. Funct. Genet. 19:1994;55-72.
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 49
    • 0028158628 scopus 로고
    • PHD-an automatic mail server for protein secondary structure
    • Rost B., Sander C., Schneider R. PHD-an automatic mail server for protein secondary structure. CABIOS. 10:1994;53-60.
    • (1994) CABIOS , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 50
    • 0032539854 scopus 로고    scopus 로고
    • Computational learning reveals coiled coil-like motifs in histidine kinase linker domains
    • Singh M., Berger B., Kim P. S., Berger J., Cochran A. Computational learning reveals coiled coil-like motifs in histidine kinase linker domains. Proc. Natl Acad. Sci. USA. 95:1998;2738-2743.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2738-2743
    • Singh, M.1    Berger, B.2    Kim, P.S.3    Berger, J.4    Cochran, A.5
  • 51
    • 0027394628 scopus 로고
    • Epimorphin is related to a new class of neuronal and yeast vesicle targetting proteins
    • Spring J., Kato M., Bernfield M. Epimorphin is related to a new class of neuronal and yeast vesicle targetting proteins. Trends Biochem. Sci. 18:1993;124-125.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 124-125
    • Spring, J.1    Kato, M.2    Bernfield, M.3
  • 52
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Angstrom resolution
    • Sutton R., Fasshauer D., Jahn R., Brünger A. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Angstrom resolution. Nature. 395:1998;347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.1    Fasshauer, D.2    Jahn, R.3    Brünger, A.4
  • 53
    • 0028091659 scopus 로고
    • Detection of conserved segments in proteins: Iterative scanning of sequence databases with alignment blocks
    • Tatusov R., Altschul S., Koonin E. Detection of conserved segments in proteins: Iterative scanning of sequence databases with alignment blocks. Proc. Natl Acad. Sci. USA. 91:1994;12091-12095.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12091-12095
    • Tatusov, R.1    Altschul, S.2    Koonin, E.3
  • 56
    • 0032568634 scopus 로고    scopus 로고
    • The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
    • Weissenhorn W., Calder L., Wharton S., Skehel J., Wiley D. The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil. Proc. Natl Acad. Sci. USA. 95:1998a;6032-6036.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.2    Wharton, S.3    Skehel, J.4    Wiley, D.5
  • 57
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissehorn W., Carfi A., Lee K., Skehel J., Wiley D. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell. 2:1998b;605-616.
    • (1998) Mol. Cell , vol.2 , pp. 605-616
    • Weissehorn, W.1    Carfi, A.2    Lee, K.3    Skehel, J.4    Wiley, D.5
  • 58
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 are potent inhibitors of virus infection
    • Wild C., Shugars D., Greenwell T., McDanal C., Matthews T. Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 are potent inhibitors of virus infection. Proc. Natl Acad. Sci. USA. 91:1994;9770-9774.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.1    Shugars, D.2    Greenwell, T.3    McDanal, C.4    Matthews, T.5
  • 59
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Ångstrom resolution
    • Wilson I., Skehel J., Wiley D. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Ångstrom resolution. Nature. 289:1981;366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.1    Skehel, J.2    Wiley, D.3
  • 60
    • 0030987407 scopus 로고    scopus 로고
    • Multicoil: A program for predicting two- And three-stranded coiled coils
    • Wolf E., Kim P. S., Berger B. Multicoil: a program for predicting two- and three-stranded coiled coils. Protein Sci. 6:1997;1179-1189.
    • (1997) Protein Sci. , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.S.2    Berger, B.3
  • 61
    • 0030245704 scopus 로고    scopus 로고
    • Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection
    • Yao Q., Compans R. Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection. Virology. 223:1996;103-112.
    • (1996) Virology , vol.223 , pp. 103-112
    • Yao, Q.1    Compans, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.