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Volumn 444, Issue 7117, 2006, Pages 383-386

Visualization of transient encounter complexes in protein-protein association

Author keywords

[No Author keywords available]

Indexed keywords

BROWNIAN MOVEMENT; COMPUTER SIMULATION; ENZYME IMMOBILIZATION; MUTAGENESIS; PERTURBATION TECHNIQUES;

EID: 33751086423     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05201     Document Type: Article
Times cited : (365)

References (28)
  • 2
    • 0029873697 scopus 로고    scopus 로고
    • Rapid electrostatically assisted association of proteins
    • Schreiber, G. & Fersht, A. R. Rapid electrostatically assisted association of proteins. Nature Struct. Biol. 3, 427-431 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 3
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • Vijaykumar, M. et al. Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar. J. Mol. Biol. 278, 1015-1024 (1998).
    • (1998) J. Mol. Biol. , vol.278 , pp. 1015-1024
    • Vijaykumar, M.1
  • 4
    • 0033923367 scopus 로고    scopus 로고
    • Rational design of faster associating and tighter binding protein complexes
    • Selzer, T., Albeck, S. & Schreiber, G. Rational design of faster associating and tighter binding protein complexes. Nature Struct. Biol. 7, 537-541 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 537-541
    • Selzer, T.1    Albeck, S.2    Schreiber, G.3
  • 5
    • 0024040620 scopus 로고
    • Brownian dynamics of cytochrome c and cytochrome c peroxidase association
    • Northrup, S. H., Boles, J. O. & Reynolds, J. C. L. Brownian dynamics of cytochrome c and cytochrome c peroxidase association. Science 241, 67-70 (1988).
    • (1988) Science , vol.241 , pp. 67-70
    • Northrup, S.H.1    Boles, J.O.2    Reynolds, J.C.L.3
  • 9
    • 19744381543 scopus 로고    scopus 로고
    • Enhancement of association rates by nonspecific binding to DNA and cell membranes
    • Zhou, H-X. & Szabo, A. Enhancement of association rates by nonspecific binding to DNA and cell membranes. Phys. Rev. Lett. 93, 178101 (2004).
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 178101
    • Zhou, H.-X.1    Szabo, A.2
  • 10
    • 0032939176 scopus 로고    scopus 로고
    • Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr
    • Garrett, D. S., Seok, Y-J., Peterkofsky, A., Gronenborn, A. M. & Clore, G. M. Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. Nature Struct. Biol. 6, 166-173 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 166-173
    • Garrett, D.S.1    Seok, Y.-J.2    Peterkofsky, A.3    Gronenborn, A.M.4    Clore, G.M.5
  • 12
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • Iwahara, J. & Clore, G. M. Detecting transient intermediates in macromolecular binding by paramagnetic NMR. Nature 440, 1227-1230 (2006).
    • (2006) Nature , vol.440 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 13
    • 5644226078 scopus 로고    scopus 로고
    • Characterization of nonspecific protein-DNA interactions by 1H paramagnetic relaxation enhancement
    • Iwahara, J., Schwieters, C. D. & Clore, G. M. Characterization of nonspecific protein-DNA interactions by 1H paramagnetic relaxation enhancement. J. Am. Chem. Soc. 126, 12800-12808 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12800-12808
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 14
    • 0026489715 scopus 로고
    • Incorporation of an EDTA-metal complex at a rationally selected site within a protein: Application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro
    • Ebright, Y. W., Chen, Y., Pendergrast, P. S. & Ebright, R. H. Incorporation of an EDTA-metal complex at a rationally selected site within a protein: application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro. Biochemistry 31, 10664-10670 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10664-10670
    • Ebright, Y.W.1    Chen, Y.2    Pendergrast, P.S.3    Ebright, R.H.4
  • 15
    • 2442433447 scopus 로고    scopus 로고
    • Ensemble approach for NMR structure refinement against 1H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecules
    • Iwahara, J., Schwieters, C. D. & Clore, G. M. Ensemble approach for NMR structure refinement against 1H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecules. J. Am. Chem. Soc. 126, 5879-5896 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5879-5896
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 16
    • 0035840960 scopus 로고    scopus 로고
    • Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy
    • Donaldson, L. W. et al. Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy. J. Am. Chem. Soc. 123, 9843-9847 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9843-9847
    • Donaldson, L.W.1
  • 17
    • 0037160426 scopus 로고    scopus 로고
    • Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate
    • Pintacuda, G. & Otting, G. Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate. J. Am. Chem. Soc. 124, 372-373 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 372-373
    • Pintacuda, G.1    Otting, G.2
  • 18
  • 19
    • 0027918891 scopus 로고
    • Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation
    • Brünger, A. T., Clore, G. M., Gronenborn, A. M. & Nilges, M. Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science 261, 328-331 (1993).
    • (1993) Science , vol.261 , pp. 328-331
    • Brünger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Nilges, M.4
  • 20
    • 0036367763 scopus 로고    scopus 로고
    • Reweighted atomic densities to represent ensembles of NMR structures
    • Schwieters, C. D. & Clore, G. M. Reweighted atomic densities to represent ensembles of NMR structures. J. Biomol. NMR 23, 221-225 (2002).
    • (2002) J. Biomol. NMR , vol.23 , pp. 221-225
    • Schwieters, C.D.1    Clore, G.M.2
  • 21
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A., Sept, D., Joseph, S., Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 22
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S. & Thornton, J. M. principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93, 13-20 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 23
    • 0036829797 scopus 로고    scopus 로고
    • Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Eschrichia coli phosphotransferase system
    • Cornilescu, G. et al. Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Eschrichia coli phosphotransferase system. J. Biol. Chem. 277, 42289-42298 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 42289-42298
    • Cornilescu, G.1
  • 24
    • 20144384787 scopus 로고    scopus 로고
    • Solution NMR structure of the 48 kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system
    • Williams, D. C., Cai, M., Suh, Y-J., Peterkofsky, A. & Clore, G. M. Solution NMR structure of the 48 kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system. J. Biol. Chem. 280, 20775-20784 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 20775-20784
    • Williams, D.C.1    Cai, M.2    Suh, Y.-J.3    Peterkofsky, A.4    Clore, G.M.5
  • 25
    • 0023998438 scopus 로고
    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints: Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
    • Nilges, M., Gronenborn, A. M., Brünger, A. T. & Clore, G. M. Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints: application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27-38 (1988).
    • (1988) Protein Eng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brünger, A.T.3    Clore, G.M.4
  • 26
    • 0033577269 scopus 로고    scopus 로고
    • Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration
    • Kuszewski, J., Gronenborn, A. M. & Clore, G. M. Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration. J. Am. Chem. Soc. 121, 2337-2338 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2337-2338
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 28
    • 0028881975 scopus 로고
    • SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions
    • Laskowski, R. A. SURFNET: a program for visualizing molecular surfaces, cavities and intermolecular interactions. J. Mol. Graph. 13, 323-330 (1995).
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.