메뉴 건너뛰기




Volumn 2, Issue 2, 2005, Pages

Overcoming residual frustration in domain-swapping: The roles of disulfide bonds in dimerization and aggregation

Author keywords

[No Author keywords available]

Indexed keywords

CYANOVIRIN N;

EID: 22244447465     PISSN: 14783967     EISSN: 14783975     Source Type: Journal    
DOI: 10.1088/1478-3975/2/2/S05     Document Type: Article
Times cited : (39)

References (43)
  • 1
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson J D and Wolynes P G 1987 Spin glasses and the statistical mechanics of protein folding Proc. Natl Acad. Sci. USA 84 7524-8
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 2
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and 'en-route' intermediates for protein folding? An investigation for small globular proteins
    • Clementi C, Nymeyer H and Onuchic J N 2000 Topological and energetic factors: what determines the structural details of the transition state ensemble and 'en-route' intermediates for protein folding? An investigation for small globular proteins J. Mol. Biol. 298 937-53
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 3
    • 0030322669 scopus 로고    scopus 로고
    • Protein folding funnels: The nature of the transition state ensemble
    • Onuchic J N, Socci N D, Luthey-Schulten Z and Wolynes P G 1996 Protein folding funnels: the nature of the transition state ensemble Fold Des. 1 441-50
    • (1996) Fold Des. , vol.1 , pp. 441-450
    • Onuchic, J.N.1    Socci, N.D.2    Luthey-Schulten, Z.3    Wolynes, P.G.4
  • 4
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Go-like model
    • Koga N and Takada S 2001 Roles of native topology and chain-length scaling in protein folding: a simulation study with a Go-like model J. Mol. Biol. 313 171-80
    • (2001) J. Mol. Biol. , vol.313 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 5
    • 3142782241 scopus 로고    scopus 로고
    • Quantifying the roughness on the free energy landscape: Entropic bottlenecks and protein folding rates
    • Chavez L L, Onuchic J N and Clementi C 2004 Quantifying the roughness on the free energy landscape: entropic bottlenecks and protein folding rates J. Am. Chem. Soc. 126 8426-32
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8426-8432
    • Chavez, L.L.1    Onuchic, J.N.2    Clementi, C.3
  • 6
    • 0034705115 scopus 로고    scopus 로고
    • How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta
    • Clementi C, Jennings P A and Onuchic J N 2000 How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta Proc. Natl Acad. Sci. USA 97 5871-6
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5871-5876
    • Clementi, C.1    Jennings, P.A.2    Onuchic, J.N.3
  • 8
    • 13444301037 scopus 로고    scopus 로고
    • A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes
    • Levy Y, Cho S S, Onuchic J N and Wolynes P G 2005 A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes J. Mol. Biol. 346 1121-45
    • (2005) J. Mol. Biol. , vol.346 , pp. 1121-1145
    • Levy, Y.1    Cho, S.S.2    Onuchic, J.N.3    Wolynes, P.G.4
  • 9
    • 4644301408 scopus 로고    scopus 로고
    • Domain swapping is a consequence of minimal frustration
    • Yang S et al 2004 Domain swapping is a consequence of minimal frustration Proc. Natl Acad. Sci. USA 101 13786-91
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13786-13791
    • Yang, S.1
  • 11
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett M J, Schlunegger M P and Eisenberg D 1995 3D domain swapping: a mechanism for oligomer assembly Protein Sci. 4 2455-68
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 12
    • 0032463747 scopus 로고    scopus 로고
    • All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly
    • Bergdoll M, Eltis L D, Cameron A D, Dumas P and Bolin J T 1998 All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly Protein Sci. 7 1661-70
    • (1998) Protein Sci. , vol.7 , pp. 1661-1670
    • Bergdoll, M.1    Eltis, L.D.2    Cameron, A.D.3    Dumas, P.4    Bolin, J.T.5
  • 13
    • 0035826713 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
    • Rousseau F, Schymkowitz J W, Wilkinson H R and Itzhaki L S 2001 Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues Proc. Natl Acad. Sci. USA 98 5596-601
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5596-5601
    • Rousseau, F.1    Schymkowitz, J.W.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 14
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu Y and Eisenberg D 2002 3D domain swapping: as domains continue to swap Protein Sci. 11 1285-99
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 15
    • 0033773675 scopus 로고    scopus 로고
    • Dimer formation by a 'monomeric' protein
    • Park C and Raines R T 2000 Dimer formation by a 'monomeric' protein Protein Sci. 9 2026-33
    • (2000) Protein Sci. , vol.9 , pp. 2026-2033
    • Park, C.1    Raines, R.T.2
  • 17
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase a dimer with implications for amyloid formation
    • Liu Y, Gotte G, Libonati M and Eisenberg D 2001 A domain-swapped RNase A dimer with implications for amyloid formation Nat Struct. Biol. 8 211-4
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 18
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger M P, Bennett M J and Eisenberg D 1997 Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly Adv. Protein Chem. 50 61-122
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 19
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen F E and Prusiner S B 1998 Pathologic conformations of prion proteins Annu. Rev. Biochem. 67 793-819
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 21
    • 0035069135 scopus 로고    scopus 로고
    • Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping
    • Janowski R et al 2001 Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping Nat. Struct. Biol. 8 316-20
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 316-320
    • Janowski, R.1
  • 23
    • 0042320356 scopus 로고    scopus 로고
    • Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process
    • Lee S and Eisenberg D 2003 Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process Nat. Struct. Biol. 10 725-30
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 725-730
    • Lee, S.1    Eisenberg, D.2
  • 24
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U and Sander C 1994 Enlarged representative set of protein structures Protein Sci. 3 522-4
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 25
    • 0036923039 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the SH3 domain aggregation suggests a generic amyloidogenesis mechanism
    • Ding F, Dokholyan N V, Buldyrev S V, Stanley H E and Shakhnovich E I 2002 Molecular dynamics simulation of the SH3 domain aggregation suggests a generic amyloidogenesis mechanism J. Mol. Biol. 324 851-7
    • (2002) J. Mol. Biol. , vol.324 , pp. 851-857
    • Ding, F.1    Dokholyan, N.V.2    Buldyrev, S.V.3    Stanley, H.E.4    Shakhnovich, E.I.5
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W and Sander C 1983 Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 2577-637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0037126686 scopus 로고    scopus 로고
    • Proline cis-trans isomerization and protein folding
    • Wedemeyer W J, Welker E and Scheraga H A 2002 Proline cis-trans isomerization and protein folding Biochemistry 41 14637-44
    • (2002) Biochemistry , vol.41 , pp. 14637-14644
    • Wedemeyer, W.J.1    Welker, E.2    Scheraga, H.A.3
  • 29
    • 17144424217 scopus 로고    scopus 로고
    • The role of the hinge loop in domain-swapping: The special case of Bovine seminal Ribonuclease
    • Picone D et al 2005 The role of the hinge loop in domain-swapping: the special case of Bovine seminal Ribonuclease J. Biol. Chem. 280 13771-8
    • (2005) J. Biol. Chem. , vol.280 , pp. 13771-13778
    • Picone, D.1
  • 30
    • 0026354773 scopus 로고
    • High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin
    • Lapatto R et al 1991 High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin J. Mol. Biol. 222 1067-83
    • (1991) J. Mol. Biol. , vol.222 , pp. 1067-1083
    • Lapatto, R.1
  • 31
    • 0000522537 scopus 로고    scopus 로고
    • Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat
    • Chen Y W, Stott K and Perutz M F 1999 Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat Proc. Natl Acad. Sci. USA 96 1257-61
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1257-1261
    • Chen, Y.W.1    Stott, K.2    Perutz, M.F.3
  • 32
    • 0000384736 scopus 로고    scopus 로고
    • Alternative explanations for 'multistate' kinetics in protein folding: Transient aggregation and changing transition-state ensembles
    • Oliveberg M 1998 Alternative explanations for 'multistate' kinetics in protein folding: transient aggregation and changing transition-state ensembles Acc. Chem. Res. 31 765-72
    • (1998) Acc. Chem. Res. , vol.31 , pp. 765-772
    • Oliveberg, M.1
  • 33
    • 0033532212 scopus 로고    scopus 로고
    • Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping
    • Yang F et al 1999 Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping J. Mol. Biol. 288 403-12
    • (1999) J. Mol. Biol. , vol.288 , pp. 403-412
    • Yang, F.1
  • 34
    • 0031559753 scopus 로고    scopus 로고
    • Analysis of sequence requirements for biological activity of cyanovirin-N, a potent HIV (human immunodeficiency virus)-inactivating protein
    • Mori T et al 1997 Analysis of sequence requirements for biological activity of cyanovirin-N, a potent HIV (human immunodeficiency virus)-inactivating protein Biochem. Biophys. Res. Commun. 238 218-22
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 218-222
    • Mori, T.1
  • 35
    • 0036113691 scopus 로고    scopus 로고
    • The domain-swapped dimer of cyanovirin-N is in a metastable folded state: Reconciliation of X-ray and NMR structures
    • Barrientos L G et al 2002 The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures Structure (Camb.) 10 673-86
    • (2002) Structure (Camb.) , vol.10 , pp. 673-686
    • Barrientos, L.G.1
  • 36
    • 4644253146 scopus 로고    scopus 로고
    • Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity
    • Barrientos L G, Lasala F, Delgado R, Sanchez A and Gronenborn A M 2004 Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity Structure (Camb.) 12 1799-807
    • (2004) Structure (Camb.) , vol.12 , pp. 1799-1807
    • Barrientos, L.G.1    Lasala, F.2    Delgado, R.3    Sanchez, A.4    Gronenborn, A.M.5
  • 37
    • 0037031950 scopus 로고    scopus 로고
    • Intramolecular versus intermolecular disulfide bonds in prion proteins
    • Welker E, Raymond L D, Scheraga H A and Caughey B 2002 Intramolecular versus intermolecular disulfide bonds in prion proteins J. Biol. Chem. 277 33477-81
    • (2002) J. Biol. Chem. , vol.277 , pp. 33477-33481
    • Welker, E.1    Raymond, L.D.2    Scheraga, H.A.3    Caughey, B.4
  • 39
  • 40
    • 0030579560 scopus 로고    scopus 로고
    • Prionics or the kinetic basis of prion diseases
    • Eigen M 1996 Prionics or the kinetic basis of prion diseases Biophys. Chem. 63 A1-18
    • (1996) Biophys. Chem. , vol.63
    • Eigen, M.1
  • 41
    • 0032968132 scopus 로고    scopus 로고
    • Quantifying the kinetic parameters of prion replication
    • Masel J, Jansen V A and Nowak M A 1999 Quantifying the kinetic parameters of prion replication Biophys. Chem. 77 139-52
    • (1999) Biophys. Chem. , vol.77 , pp. 139-152
    • Masel, J.1    Jansen, V.A.2    Nowak, M.A.3
  • 42
    • 0034699419 scopus 로고    scopus 로고
    • Thiol-disulfide interchange a potential key to conformational change associated with amyloid fibril formation
    • Feughelman M and Willis B K 2000 Thiol-disulfide interchange a potential key to conformational change associated with amyloid fibril formation J. Theor. Biol. 206 313-5
    • (2000) J. Theor. Biol. , vol.206 , pp. 313-315
    • Feughelman, M.1    Willis, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.