메뉴 건너뛰기




Volumn 382, Issue 1, 2008, Pages 223-235

Mechanism and Energy Landscape of Domain Swapping in the B1 Domain of Protein G

Author keywords

domain swapping; encounter complex; protein interactions

Indexed keywords

BINDING PROTEIN; DIMER; IMMUNOGLOBULIN G; MONOMER; OLIGOMER; POLYPEPTIDE; PROTEIN G;

EID: 49349104659     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.06.025     Document Type: Article
Times cited : (30)

References (38)
  • 1
    • 0028865843 scopus 로고
    • 3D domain swapping: a mechanism for oligomer assembly
    • Bennett M.J., Schlunegger M.P., and Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci 4 (1995) 2455-2468
    • (1995) Protein Sci , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 2
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: as domains continue to swap
    • Liu Y., and Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci. 11 (2002) 1285
    • (2002) Protein Sci. , vol.11 , pp. 1285
    • Liu, Y.1    Eisenberg, D.2
  • 3
    • 33646375442 scopus 로고    scopus 로고
    • Deposition diseases and 3D domain swapping
    • Bennett M.J., Sawaya M.R., and Eisenberg D. Deposition diseases and 3D domain swapping. Structure 14 (2006) 811-824
    • (2006) Structure , vol.14 , pp. 811-824
    • Bennett, M.J.1    Sawaya, M.R.2    Eisenberg, D.3
  • 4
    • 0347914553 scopus 로고    scopus 로고
    • Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR
    • Ding K., Louis J.M., and Gronenborn A.M. Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR. J. Mol. Biol. 335 (2004) 1299-1307
    • (2004) J. Mol. Biol. , vol.335 , pp. 1299-1307
    • Ding, K.1    Louis, J.M.2    Gronenborn, A.M.3
  • 6
    • 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.H., Wilkinson H.R., and Itzhaki L.S. Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proc. Natl Acad. Sci. USA 98 (2001) 5596
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5596
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 9
    • 0037337270 scopus 로고    scopus 로고
    • The unfolding story of three-dimensional domain swapping
    • Rousseau F., Schymkowitz J.W.H., and Itzhaki L.S. The unfolding story of three-dimensional domain swapping. Structure 11 (2003) 243-251
    • (2003) Structure , vol.11 , pp. 243-251
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Itzhaki, L.S.3
  • 10
    • 0022545967 scopus 로고
    • Gene for an immunoglobulin-binding protein from a group G streptococcus
    • Fahnestock S.R., Alexander P., Nagle J., and Filpula D. Gene for an immunoglobulin-binding protein from a group G streptococcus. J. Bacteriol. 167 (1986) 870-880
    • (1986) J. Bacteriol. , vol.167 , pp. 870-880
    • Fahnestock, S.R.1    Alexander, P.2    Nagle, J.3    Filpula, D.4
  • 11
    • 0141569110 scopus 로고    scopus 로고
    • A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping
    • Byeon I.J., Louis J.M., and Gronenborn A.M. A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping. J. Mol. Biol. 333 (2003) 141-152
    • (2003) J. Mol. Biol. , vol.333 , pp. 141-152
    • Byeon, I.J.1    Louis, J.M.2    Gronenborn, A.M.3
  • 13
    • 2942755921 scopus 로고    scopus 로고
    • A captured folding intermediate involved in dimerization and domain-swapping of GB1
    • Byeon I.J., Louis J.M., and Gronenborn A.M. A captured folding intermediate involved in dimerization and domain-swapping of GB1. J. Mol. Biol. 340 (2004) 615-625
    • (2004) J. Mol. Biol. , vol.340 , pp. 615-625
    • Byeon, I.J.1    Louis, J.M.2    Gronenborn, A.M.3
  • 14
    • 17144382523 scopus 로고    scopus 로고
    • The GB1 amyloid fibril: recruitment of the peripheral beta-strands of the domain swapped dimer into the polymeric interface
    • Louis J.M., Byeon I.J., Baxa U., and Gronenborn A.M. The GB1 amyloid fibril: recruitment of the peripheral beta-strands of the domain swapped dimer into the polymeric interface. J. Mol. Biol. 348 (2005) 687-698
    • (2005) J. Mol. Biol. , vol.348 , pp. 687-698
    • Louis, J.M.1    Byeon, I.J.2    Baxa, U.3    Gronenborn, A.M.4
  • 15
    • 0041810451 scopus 로고    scopus 로고
    • Efficient exploration of reactive potential energy surfaces using Car-Parrinello molecular dynamics
    • Iannuzzi M., Laio A., and Parrinello M. Efficient exploration of reactive potential energy surfaces using Car-Parrinello molecular dynamics. Phys. Rev. Lett. 90 (2003) 238302
    • (2003) Phys. Rev. Lett. , vol.90 , pp. 238302
    • Iannuzzi, M.1    Laio, A.2    Parrinello, M.3
  • 16
    • 0000191981 scopus 로고
    • Reaction path study of conformational transitions in flexible systems: applications to peptides
    • Czerminski R., and Elber R. Reaction path study of conformational transitions in flexible systems: applications to peptides. J. Chem. Phys. 92 (1990) 5580
    • (1990) J. Chem. Phys. , vol.92 , pp. 5580
    • Czerminski, R.1    Elber, R.2
  • 17
    • 0028204771 scopus 로고
    • Domain swapping: entangling alliances between proteins
    • Bennett M.J., Choe S., and Eisenberg D. Domain swapping: entangling alliances between proteins. Proc. Natl Acad. Sci. USA 91 (1994) 3127-3131
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 18
    • 44949109198 scopus 로고    scopus 로고
    • Role of the amino acid sequence in domain swapping of the B1 domain of protein G
    • Sirota F.L., Hery-Huynh S., Maurer-Stroh S., and Wodak S.J. Role of the amino acid sequence in domain swapping of the B1 domain of protein G. Proteins 72 (2008) 88-104
    • (2008) Proteins , vol.72 , pp. 88-104
    • Sirota, F.L.1    Hery-Huynh, S.2    Maurer-Stroh, S.3    Wodak, S.J.4
  • 19
    • 36749006579 scopus 로고    scopus 로고
    • Lensink, M. F., Mendez, R. & Wodak, S. J. (2007). Docking and Scoring Protein Complexes: CAPRI, 3rd edit. Proteins, 69, 704-718.
    • Lensink, M. F., Mendez, R. & Wodak, S. J. (2007). Docking and Scoring Protein Complexes: CAPRI, 3rd edit. Proteins, 69, 704-718.
  • 20
    • 19944406574 scopus 로고
    • Dynamics of entangled polymer solutions: I. The Rouse model
    • De Gennes P.G. Dynamics of entangled polymer solutions: I. The Rouse model. Macromolecules 9 (1976) 587-593
    • (1976) Macromolecules , vol.9 , pp. 587-593
    • De Gennes, P.G.1
  • 21
  • 22
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47 (1995) 83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 23
    • 0034682869 scopus 로고    scopus 로고
    • Automatic protein design with all atom force-fields by exact and heuristic optimization
    • Wernisch L., Hery S., and Wodak S.J. Automatic protein design with all atom force-fields by exact and heuristic optimization. J. Mol. Biol. 301 (2000) 713-736
    • (2000) J. Mol. Biol. , vol.301 , pp. 713-736
    • Wernisch, L.1    Hery, S.2    Wodak, S.J.3
  • 25
    • 0032867418 scopus 로고    scopus 로고
    • Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing
    • Park S.H., Shastry M.C., and Roder H. Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing. Nat. Struct. Biol. 6 (1999) 943-947
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 943-947
    • Park, S.H.1    Shastry, M.C.2    Roder, H.3
  • 26
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable bold beta-hairpin in aqueous solution
    • Blanco F.J., Rivas G., and Serrano L. A short linear peptide that folds into a native stable bold beta-hairpin in aqueous solution. Nat. Struct. Biol. 1 (1994) 584-590
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 27
    • 0028877368 scopus 로고
    • Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch
    • Bourne Y., Arvai A.S., Bernstein S.L., Watson M.H., Reed S.I., Endicott J.E., et al. Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch. Proc. Natl Acad. Sci. USA 92 (1995) 10232-10236
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10232-10236
    • Bourne, Y.1    Arvai, A.S.2    Bernstein, S.L.3    Watson, M.H.4    Reed, S.I.5    Endicott, J.E.6
  • 28
    • 0035190116 scopus 로고    scopus 로고
    • Single-site mutations induce 3D domain swapping in the B1 domain of protein l from Peptostreptococcus magnus
    • O'Neill J.W., Kim D.E., Johnsen K., Baker D., and Zhang K.Y.J. Single-site mutations induce 3D domain swapping in the B1 domain of protein l from Peptostreptococcus magnus. Structure 9 (2001) 1017-1027
    • (2001) Structure , vol.9 , pp. 1017-1027
    • O'Neill, J.W.1    Kim, D.E.2    Johnsen, K.3    Baker, D.4    Zhang, K.Y.J.5
  • 30
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • Wodak S.J., and Janin J. Structural basis of macromolecular recognition. Adv. Protein Chem. 61 (2002) 9-73
    • (2002) Adv. Protein Chem. , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 33
    • 0026511656 scopus 로고
    • The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht A.R., Matouschek A., and Serrano L. The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224 (1992) 771-782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 34
    • 0001563899 scopus 로고
    • Free-energy of ionic hydration-analysis of a thermodynamic integration technique to evaluate free-energy differences by molecular-dynamics simulations
    • Straatsma T.P., and Berendsen H.J.C. Free-energy of ionic hydration-analysis of a thermodynamic integration technique to evaluate free-energy differences by molecular-dynamics simulations. J. Chem. Phys. 89 (1988) 5876-5886
    • (1988) J. Chem. Phys. , vol.89 , pp. 5876-5886
    • Straatsma, T.P.1    Berendsen, H.J.C.2
  • 36
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis T., and Karplus M. Effective energy function for proteins in solution. Proteins: Struct. Funct. Genet. 35 (1999) 133-152
    • (1999) Proteins: Struct. Funct. Genet. , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 37
    • 0141956090 scopus 로고    scopus 로고
    • Generalized Born model with a simple smoothing function
    • Im W., Lee M.S., and Brooks III C.L. Generalized Born model with a simple smoothing function. J. Comput. Chem. 24 (2003) 1691-1702
    • (2003) J. Comput. Chem. , vol.24 , pp. 1691-1702
    • Im, W.1    Lee, M.S.2    Brooks III, C.L.3
  • 38
    • 0023338543 scopus 로고
    • Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides
    • Ooi T., Oobatake M., Nemethy G., and Scheraga H.A. Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides. Proc. Natl Acad. Sci. USA 84 (1987) 3086-3090
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3086-3090
    • Ooi, T.1    Oobatake, M.2    Nemethy, G.3    Scheraga, H.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.