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Volumn 11, Issue 12, 2002, Pages 2792-2803

The interaction of β2-glycoprotein I domain V with chaperonin GroEL: The similarity with the domain V and membrane interaction

Author keywords

2 Glycoprotein I; Chaperonin GroEL; Disulfide bond reduction; H 2H exchange; Heteronuclear NMR

Indexed keywords

AMIDE; BETA2 GLYCOPROTEIN 1; CHAPERONIN; DISULFIDE; GLYCOPROTEIN; HYDROGEN; MEMBRANE PROTEIN; PROTON; TRYPTOPHAN;

EID: 0036892448     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0216602     Document Type: Article
Times cited : (3)

References (47)
  • 1
  • 3
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig, K., Adams, P.D., and Brünger, A.T. 1995. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat. Struct. Biol. 2: 1083-1094.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 5
    • 0030966765 scopus 로고    scopus 로고
    • A structural model for GroELpolypeptide recognition
    • Buckle, A.M., Zahn, R., and Fersht, A.R. 1997. A structural model for GroELpolypeptide recognition. Proc. Natl. Acad. Sci. 94: 3571-3575.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 3571-3575
    • Buckle, A.M.1    Zahn, R.2    Fersht, A.R.3
  • 6
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp 70 and Hsp 60 chaperone machines
    • Bukau, B. and Horwich, A.L. 1998. The Hsp 70 and Hsp 60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 7
    • 0034671267 scopus 로고    scopus 로고
    • From mini chaperone to GroEL 2: Importance of avidity of the multisite ring structure
    • Chatellier, J., Hill, F., and Fersht, A.R. 2000a. From mini chaperone to GroEL 2: Importance of avidity of the multisite ring structure. J. Mol. Biol. 304: 883-896.
    • (2000) J. Mol. Biol. , vol.304 , pp. 883-896
    • Chatellier, J.1    Hill, F.2    Fersht, A.R.3
  • 8
    • 0034671453 scopus 로고    scopus 로고
    • From minichaperone to GroEL 3: Properties of an active single-ring mutant of GroEL
    • Chatellier, J., Hill, F., Foster, N.W., Goloubinoff, P., and Fersht, A.R. 2000b. From minichaperone to GroEL 3: Properties of an active single-ring mutant of GroEL. J. Mol. Biol. 304: 897-910.
    • (2000) J. Mol. Biol. , vol.304 , pp. 897-910
    • Chatellier, J.1    Hill, F.2    Foster, N.W.3    Goloubinoff, P.4    Fersht, A.R.5
  • 9
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • Chen, L. and Sigler, P.B. 1999. The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity. Cell 99: 757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 10
    • 0031918147 scopus 로고    scopus 로고
    • Purification of GroEL with low fluorescence background
    • Clark, A.C., Ramanathan, R., and Friden, C. 1998. Purification of GroEL with low fluorescence background. Methods Enzymol. 290: 100-118.
    • (1998) Methods Enzymol. , vol.290 , pp. 100-118
    • Clark, A.C.1    Ramanathan, R.2    Friden, C.3
  • 12
    • 0031297406 scopus 로고    scopus 로고
    • Structural and mechanistic consequence of polypeptide binding by GroEL
    • Coyle, J.E., Jaeger, J., Gross, M., Robinson, C.V., and Radford, S.E. 1997. Structural and mechanistic consequence of polypeptide binding by GroEL. Fold. Des. 2: R93-R104.
    • (1997) Fold. Des. , vol.2
    • Coyle, J.E.1    Jaeger, J.2    Gross, M.3    Robinson, C.V.4    Radford, S.E.5
  • 14
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax. A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 15
    • 0034972451 scopus 로고    scopus 로고
    • Structural changes in GroEL effected by binding a denatured protein substrate
    • Falke, S., Fisher, M.T., and Gogol, E.P. 2001. Structural changes in GroEL effected by binding a denatured protein substrate. J. Mol. Biol. 308: 569-577.
    • (2001) J. Mol. Biol. , vol.308 , pp. 569-577
    • Falke, S.1    Fisher, M.T.2    Gogol, E.P.3
  • 16
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton, W.A. and Horwich, A.L. 1997. GroEL-mediated protein folding. Protein Sci. 6: 743-760.
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 18
    • 0032548994 scopus 로고    scopus 로고
    • Thermodynamic stability and folding of GroEL minichaperones
    • Golbik, R., Zahn, R., Harding, S.E., and Fersht, A.R. 1998. Thermodynamic stability and folding of GroEL minichaperones. J. Mol. Biol. 276: 505-515.
    • (1998) J. Mol. Biol. , vol.276 , pp. 505-515
    • Golbik, R.1    Zahn, R.2    Harding, S.E.3    Fersht, A.R.4
  • 21
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. 2002. Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295: 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 22
    • 0035799334 scopus 로고    scopus 로고
    • Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif
    • Hinderliter, A., Almeida, P.F., Creutz, C.E., and Biltonen, R.L. 2001. Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif. Biochemistry 40: 4181-4191.
    • (2001) Biochemistry , vol.40 , pp. 4181-4191
    • Hinderliter, A.1    Almeida, P.F.2    Creutz, C.E.3    Biltonen, R.L.4
  • 23
    • 0035838472 scopus 로고    scopus 로고
    • 2glycoprotein I domain V specifically interacts with hydrophobic ligands
    • 2glycoprotein I domain V specifically interacts with hydrophobic ligands. Biochemistry 40: 8092-8100.
    • (2001) Biochemistry , vol.40 , pp. 8092-8100
    • Hong, D.P.1    Hagihara, Y.2    Kato, H.3    Goto, Y.4
  • 24
    • 0030569019 scopus 로고    scopus 로고
    • Interaction of GroEL with conformational states of horse cytochrome c
    • Hoshino, M., Kawata, Y., and Goto, Y. 1996. Interaction of GroEL with conformational states of horse cytochrome c. J. Mol. Biol. 262: 575-587.
    • (1996) J. Mol. Biol. , vol.262 , pp. 575-587
    • Hoshino, M.1    Kawata, Y.2    Goto, Y.3
  • 26
    • 0027522834 scopus 로고
    • 2-glycoprotein I critical for lipid-binding and anticardiolipin antibody cofactor activity
    • 2-glycoprotein I critical for lipid-binding and anticardiolipin antibody cofactor activity. Proc. Natl. Acad. Sci. 90: 2141-2145.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 2141-2145
    • Hunt, J.E.1    Simpson, R.J.2    Krilis, S.A.3
  • 27
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of a-lactalbumin by GroEL
    • Katsumata, K., Okazaki, A., Tsurupa, G.P., and Kuwajima, K. 1996. Dominant forces in the recognition of a transient folding intermediate of a-lactalbumin by GroEL. J. Mol. Biol. 264: 643-649.
    • (1996) J. Mol. Biol. , vol.264 , pp. 643-649
    • Katsumata, K.1    Okazaki, A.2    Tsurupa, G.P.3    Kuwajima, K.4
  • 28
    • 0032436175 scopus 로고    scopus 로고
    • Chaperonin GroEfacilitated refolding of disulfide-bonded and reduced taka-amylase A from Aspergillus oryzae
    • Kawata, Y., Hongo, K., Mizobata, T., and Nagai, J. 1998. Chaperonin GroEfacilitated refolding of disulfide-bonded and reduced taka-amylase A from Aspergillus oryzae. Protein Eng. 11: 1293-1298.
    • (1998) Protein Eng. , vol.11 , pp. 1293-1298
    • Kawata, Y.1    Hongo, K.2    Mizobata, T.3    Nagai, J.4
  • 29
    • 0033619703 scopus 로고    scopus 로고
    • Functional communications between the apical and equatorial domains of GroEL through the intermediate domain
    • Kawata, Y., Kawagoe, M., Hongo, K., Miyazaki, T., Higurashi, T., Mizobata, T., and Nagai, J. 1999. Functional communications between the apical and equatorial domains of GroEL through the intermediate domain. Biochemistry 38: 15732-15740.
    • (1999) Biochemistry , vol.38 , pp. 15732-15740
    • Kawata, Y.1    Kawagoe, M.2    Hongo, K.3    Miyazaki, T.4    Higurashi, T.5    Mizobata, T.6    Nagai, J.7
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0034665864 scopus 로고    scopus 로고
    • A dynamic model for the allosteric mechanism of GroEL
    • Ma, J., Sigler, P.B., Xu, Z., and Karplus, M. 2000. A dynamic model for the allosteric mechanism of GroEL. J. Mol. Biol. 302: 303-313.
    • (2000) J. Mol. Biol. , vol.302 , pp. 303-313
    • Ma, J.1    Sigler, P.B.2    Xu, Z.3    Karplus, M.4
  • 33
    • 0031554905 scopus 로고    scopus 로고
    • Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR
    • Nieba-Axmann, S.E., Ottiger, M., Wüthrich, K., and Plückthun, A. 1997. Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR. J. Mol. Biol. 271: 803-818.
    • (1997) J. Mol. Biol. , vol.271 , pp. 803-818
    • Nieba-Axmann, S.E.1    Ottiger, M.2    Wüthrich, K.3    Plückthun, A.4
  • 34
    • 0018890403 scopus 로고
    • 2-glycoprotein I in the rat: Isolation from serum and demonstrated in lipoprotein density fractions
    • 2-glycoprotein I in the rat: Isolation from serum and demonstrated in lipoprotein density fractions. Int. J. Biochem. 11: 265-270.
    • (1980) Int. J. Biochem. , vol.11 , pp. 265-270
    • Polz, E.1    Wurm, H.2    Kostner, G.M.3
  • 37
    • 0023814733 scopus 로고    scopus 로고
    • 2-glycoprotein I on the dextran sulfate activation of the contact system (Hageman factor system) in the blood coagulation
    • 2-glycoprotein I on the dextran sulfate activation of the contact system (Hageman factor system) in the blood coagulation. Int. J. Biochem. 20: 787-792.
    • (1998) Int. J. Biochem. , vol.20 , pp. 787-792
    • Schousboe, I.1    Rasmussen, M.S.2
  • 38
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • Shtilerman, M., Lorimer, G.H., and Englander, S.W. 1999. Chaperonin function: Folding by forced unfolding. Science 284: 821-825.
    • (1999) Science , vol.284 , pp. 821-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 39
    • 0035836456 scopus 로고    scopus 로고
    • The binding of Bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL
    • Smoot, A.L., Panda, M., Brazil, B.T., Buckle, B.T., Fersht, A.R., and Horowitz, P.M. 2001. The binding of Bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL. Biochemistry 40: 4484-4492.
    • (2001) Biochemistry , vol.40 , pp. 4484-4492
    • Smoot, A.L.1    Panda, M.2    Brazil, B.T.3    Buckle, B.T.4    Fersht, A.R.5    Horowitz, P.M.6
  • 41
    • 0034876666 scopus 로고    scopus 로고
    • Single-molecule observation of protein-protein interactions in the chaperonin system
    • Taguchi, H., Ueno, T., Tadakuma, H., Yoshida, M., and Funatsu, T. 2001. Single-molecule observation of protein-protein interactions in the chaperonin system. Nat. Biotechnol. 19: 861-865.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 861-865
    • Taguchi, H.1    Ueno, T.2    Tadakuma, H.3    Yoshida, M.4    Funatsu, T.5
  • 42
    • 0034671446 scopus 로고    scopus 로고
    • From minichaperone to GroEL I: Information on GroEL-polypeptide interactions form crystal packing of minichaperones
    • Wang, Q., Buckle, A.M., and Fersht, A.R. 2000. From minichaperone to GroEL I: Information on GroEL-polypeptide interactions form crystal packing of minichaperones. J. Mol. Biol. 304: 873-881.
    • (2000) J. Mol. Biol. , vol.304 , pp. 873-881
    • Wang, Q.1    Buckle, A.M.2    Fersht, A.R.3
  • 43
    • 0021265066 scopus 로고
    • 2-glycoprotein I (apolipoprotein H) interactions with phosphlipid vesicles
    • 2-glycoprotein I (apolipoprotein H) interactions with phosphlipid vesicles. Int. J. Biochem. 16: 511-515.
    • (1984) Int. J. Biochem. , vol.16 , pp. 511-515
    • Wurm, H.1
  • 44
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GoES-(ADP)7 chaperonin complex
    • Xu, Z., Horwich, A.L., and Sigler, P.B. 1997. The crystal structure of the asymmetric GroEL-GoES-(ADP)7 chaperonin complex. Nature 388: 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 46
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • Zahn, R., Spitzfaden, C., Ottiger, M., Wüthrich, K., and Plückthun, A. 1994. Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature 368: 261-265.
    • (1994) Nature , vol.368 , pp. 261-265
    • Zahn, R.1    Spitzfaden, C.2    Ottiger, M.3    Wüthrich, K.4    Plückthun, A.5
  • 47
    • 0030061845 scopus 로고    scopus 로고
    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • Zahn, R., Perrett, S., Stenberg, G., and Fersht, A.L. 1996. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science 271: 642-645.
    • (1996) Science , vol.271 , pp. 642-645
    • Zahn, R.1    Perrett, S.2    Stenberg, G.3    Fersht, A.L.4


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