메뉴 건너뛰기




Volumn 336, Issue 1, 2004, Pages 1-8

Fast Folding of the HIV-1 and SIV gp41 Six-helix Bundles

Author keywords

Folding kinetics; Gp41; HIV 1 fusion; Six helix bundle; Trimer of hairpins motif

Indexed keywords

GLYCOPROTEIN GP 41; ISOLEUCINE; THREONINE; VIRUS FUSION PROTEIN;

EID: 0345869718     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.058     Document Type: Article
Times cited : (21)

References (28)
  • 1
    • 0021997051 scopus 로고
    • Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III
    • Allan J.S., Coligan J.E., Barin F., McLane M.F., Sodroski J.G., Rosen C.A., et al. Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III. Science. 228:1985;1091-1094.
    • (1985) Science , vol.228 , pp. 1091-1094
    • Allan, J.S.1    Coligan, J.E.2    Barin, F.3    McLane, M.F.4    Sodroski, J.G.5    Rosen, C.A.6
  • 2
    • 0021833513 scopus 로고
    • Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients
    • Robey W.G., Safai B., Oroszlan S., Arthur L.O., Gonda M.A., Gallo R.C., Fischinger P.J. Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients. Science. 228:1985;593-595.
    • (1985) Science , vol.228 , pp. 593-595
    • Robey, W.G.1    Safai, B.2    Oroszlan, S.3    Arthur, L.O.4    Gonda, M.A.5    Gallo, R.C.6    Fischinger, P.J.7
  • 3
    • 0036719574 scopus 로고    scopus 로고
    • Antibodies, viruses and vaccines
    • Burton D.R. Antibodies, viruses and vaccines. Nature Rev. Immunol. 2:2002;706-713.
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 706-713
    • Burton, D.R.1
  • 4
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Ann. Rev. Biochem. 70:2001;777-810.
    • (2001) Ann. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 5
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M., Blacklow S.C., 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.C.2    Kim, P.S.3
  • 6
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., 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.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 8
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K., Liu J., Wang J., Shen S., Lu M. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl Acad. Sci. USA. 94:1997;12303-12308.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 9
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M., Moore J.P., Furman C., Charles M., Ho D.D., Robinson J., Sodroski J. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67:1993;3978-3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 10
    • 0027488547 scopus 로고
    • Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding
    • Sattentau Q.J., Moore J.P., Vignaux F., Traincard F., Poignard P. Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding. J. Virol. 67:1993;7383-7393.
    • (1993) J. Virol. , vol.67 , pp. 7383-7393
    • Sattentau, Q.J.1    Moore, J.P.2    Vignaux, F.3    Traincard, F.4    Poignard, P.5
  • 11
    • 16144365317 scopus 로고    scopus 로고
    • CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5
    • Trkola A., Dragic T., Arthos J., Binley J.M., Olson W.C., Allaway G.P., et al. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature. 384:1996;184-187.
    • (1996) Nature , vol.384 , pp. 184-187
    • Trkola, A.1    Dragic, T.2    Arthos, J.3    Binley, J.M.4    Olson, W.C.5    Allaway, G.P.6
  • 12
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • (erratum appears in Nature Struct. Biol. (1998) 5, 612)
    • Furuta R.A., Wild C.T., Weng Y., Weiss C.D. Capture of an early fusion-active conformation of HIV-1 gp41. Nature Struct. Biol. 5:1998;276-279. (erratum appears in Nature Struct. Biol. (1998) 5, 612).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 13
    • 0031962175 scopus 로고    scopus 로고
    • Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors
    • Jones P.L., Korte T., Blumenthal R. Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors. J. Biol. Chem. 273:1998;404-409.
    • (1998) J. Biol. Chem. , vol.273 , pp. 404-409
    • Jones, P.L.1    Korte, T.2    Blumenthal, R.3
  • 14
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso I., Durell S., Sakaguchi K., Appella E., Blumenthal R. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J. Cell Biol. 140:1998;315-323.
    • (1998) J. Cell Biol. , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 15
    • 0036633932 scopus 로고    scopus 로고
    • Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state
    • Follis K.E., Larson S.J., Lu M., Nunberg J.H. Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state. J. Virol. 76:2002;7356-7362.
    • (2002) J. Virol. , vol.76 , pp. 7356-7362
    • Follis, K.E.1    Larson, S.J.2    Lu, M.3    Nunberg, J.H.4
  • 16
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion [comment]
    • Melikyan G.B., Markosyan R.M., Hemmati H., Delmedico M.K., Lambert D.M., Cohen F.S. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion [comment]. J. Cell Biol. 151:2000;413-423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 17
    • 0035937255 scopus 로고    scopus 로고
    • Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein
    • Jelesarov I., Lu M. Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein. J. Mol. Biol. 307:2001;637-656.
    • (2001) J. Mol. Biol. , vol.307 , pp. 637-656
    • Jelesarov, I.1    Lu, M.2
  • 18
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Advan. Protein Chem. 23:1968;121-282.
    • (1968) Advan. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 19
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic P. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237:1996;260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 20
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Advan. Protein Chem. 24:1970;1-95.
    • (1970) Advan. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 21
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson S.E. How do small single-domain proteins fold? Fold. Des. 3:1998;R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 22
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht A.R. Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. Proc. Natl Acad. Sci. USA. 97:1999;1525-1529.
    • (1999) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 23
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild C.T., Shugars D.C., Greenwell T.K., McDanal C.B., Matthews T.J. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 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.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 24
    • 0037059049 scopus 로고    scopus 로고
    • Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics
    • Reeves J.D., Gallo S.A., Ahmad N., Miamidian J.L., Harvey P.E., Sharron M., et al. Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc. Natl Acad. Sci. USA. 99:2002;16249-16254.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16249-16254
    • Reeves, J.D.1    Gallo, S.A.2    Ahmad, N.3    Miamidian, J.L.4    Harvey, P.E.5    Sharron, M.6
  • 25
    • 0036278546 scopus 로고    scopus 로고
    • Dissection of human immunodeficiency virus type 1 with neutralizing antibodies to gp41 fusion intermediates
    • Golding H., Zeitzeva M., de Rosny E., King L.R., Manischewitz J., Sidoeov I., et al. Dissection of human immunodeficiency virus type 1 with neutralizing antibodies to gp41 fusion intermediates. J. Virol. 76:2002;6780-6790.
    • (2002) J. Virol. , vol.76 , pp. 6780-6790
    • Golding, H.1    Zeitzeva, M.2    De Rosny, E.3    King, L.R.4    Manischewitz, J.5    Sidoeov, I.6
  • 26
    • 0035900003 scopus 로고    scopus 로고
    • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process
    • Gallo S.A., Puri A., Blumenthal R. HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process. Biochemistry. 40:2001;12231-12236.
    • (2001) Biochemistry , vol.40 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 27
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay J.W., Roberts S.J., Brody B., Hunter E. Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66:1992;4748-4756.
    • (1992) J. Virol. , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 28
    • 0032899254 scopus 로고    scopus 로고
    • Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: Implications for viral membrane fusion
    • Lu M., Ji H., Shen S. Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: implications for viral membrane fusion. J. Virol. 73:1999;4433-4438.
    • (1999) J. Virol. , vol.73 , pp. 4433-4438
    • Lu, M.1    Ji, H.2    Shen, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.