메뉴 건너뛰기




Volumn 326, Issue , 2012, Pages 35-46

NMR as a unique tool in assessment and complex determination of weak protein-protein interactions

Author keywords

Chemical shifts; NMR; NOE; PCS; PRE; RDC

Indexed keywords

PROTEIN;

EID: 84859920253     PISSN: 03401022     EISSN: None     Source Type: Book Series    
DOI: 10.1007/128_2011_216     Document Type: Review
Times cited : (48)

References (46)
  • 1
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin AC, BoscheMet al (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415(6868): 141-147
    • (2002) Nature , vol.415 , Issue.6868 , pp. 141-147
    • Gavin, A.C.1    Al, B.2
  • 3
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • DOI 10.1093/emboj/cdg359
    • Nooren IM, Thornton JM (2003) Diversity of protein-protein interactions. EMBO J 22(14): 3486-3492 (Pubitemid 36898326)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 4
    • 77957771797 scopus 로고    scopus 로고
    • Transient protein-protein interactions: Structural, functional, and network properties
    • Perkins JR, Diboun I et al (2010) Transient protein-protein interactions: structural, functional, and network properties. Structure 18(10): 1233-1243
    • (2010) Structure , vol.18 , Issue.10 , pp. 1233-1243
    • Perkins, J.R.1    Diboun, I.2
  • 5
    • 8444232122 scopus 로고    scopus 로고
    • Transient complexes of redox proteins: Structural and dynamic details from NMR studies
    • DOI 10.1002/jmr.686
    • Prudencio M, Ubbink M (2004) Transient complexes of redox proteins: structural and dynamic details from NMR studies. J Mol Recognit 17(6): 524-539 (Pubitemid 39484220)
    • (2004) Journal of Molecular Recognition , vol.17 , Issue.6 , pp. 524-539
    • Prudencio, M.1    Ubbink, M.2
  • 6
    • 73249139292 scopus 로고    scopus 로고
    • The structural analysis of protein-protein interactions by NMR spectroscopy
    • O'Connell MR, Gamsjaeger R et al (2009) The structural analysis of protein-protein interactions by NMR spectroscopy. Proteomics 9(23): 5224-5232
    • (2009) Proteomics , vol.9 , Issue.23 , pp. 5224-5232
    • O'connell, M.R.1    Gamsjaeger, R.2
  • 7
    • 0034919312 scopus 로고    scopus 로고
    • Protein-protein interactions probed by nuclear magnetic resonance spectroscopy
    • DOI 10.1016/S0076-6879(01)39323-0
    • Qin J, Vinogradova O et al (2001) Protein-protein interactions probed by nuclear magnetic resonance spectroscopy. Meth Enzymol 339: 377-389 (Pubitemid 32666570)
    • (2001) Methods in Enzymology , vol.339 , pp. 377-389
    • Qin, J.1    Vinogradova, O.2    Gronenborn, A.M.3
  • 8
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • DOI 10.1021/bi011870b
    • Zuiderweg ER (2002) Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41(1): 1-7 (Pubitemid 34049375)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 1-7
    • Zuiderweg, E.R.P.1
  • 10
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by NMR
    • DOI 10.1016/S0167-7799(97)01135-9
    • Clore GM, Gronenborn AM (1998) Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol 16(1): 22-34 (Pubitemid 28064815)
    • (1998) Trends in Biotechnology , vol.16 , Issue.1 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 12
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K, Riek R et al (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA 94(23): 12366-12371
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.23 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2
  • 15
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein- protein complexes
    • DOI 10.1038/73331
    • Takahashi H, Nakanishi T et al (2000) A novel NMR method for determining the interfaces of large protein-protein complexes. Nat Struct Biol 7(3): 220-223 (Pubitemid 30140768)
    • (2000) Nature Structural Biology , vol.7 , Issue.3 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 16
    • 0000393431 scopus 로고
    • The two-dimensional transferred nuclear Overhauser effect
    • Clore GM, Gronenborn AM (1982) The two-dimensional transferred nuclear Overhauser effect. J Magn Reson 48: 402-417
    • (1982) J Magn Reson , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 17
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacterio-phage l N-peptide/boxB RNA complex
    • Zwahlen C, Legault P et al (1997) Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacterio-phage l N-peptide/boxB RNA complex. J Am Chem Soc 119: 711-721
    • (1997) J Am Chem Soc , vol.119 , pp. 711-721
    • Zwahlen, C.1    Legault, P.2
  • 18
    • 13944249955 scopus 로고    scopus 로고
    • Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility
    • DOI 10.1016/j.molcel.2004.12.031
    • Vaynberg J, Fukuda T et al (2005) Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility. Mol Cell 17(4): 513-523 (Pubitemid 40269116)
    • (2005) Molecular Cell , vol.17 , Issue.4 , pp. 513-523
    • Vaynberg, J.1    Fukuda, T.2    Chen, K.3    Vinogradova, O.4    Velyvis, A.5    Tu, Y.6    Ng, L.7    Wu, C.8    Qin, J.9
  • 19
    • 0001050734 scopus 로고    scopus 로고
    • A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry
    • Walters KJ, Matsuo H et al. (1997) A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry. J Am Chem Soc 119: 5958-5959
    • (1997) J Am Chem Soc , vol.119 , pp. 5958-5959
    • Walters, K.J.1    Matsuo, H.2
  • 20
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • DOI 10.1016/S0076-6879(01)39313-8
    • Bax A, Kontaxis G et al (2001) Dipolar couplings in macromolecular structure determination. Meth Enzymol 339: 127-174 (Pubitemid 32666560)
    • (2001) Methods in Enzymology , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 21
    • 4344648452 scopus 로고    scopus 로고
    • Residual dipolar couplings in structure determination of biomolecules
    • Prestegard JH, Bougault CM et al (2004) Residual dipolar couplings in structure determination of biomolecules. Chem Rev 104(8): 3519-3540
    • (2004) Chem Rev , vol.104 , Issue.8 , pp. 3519-3540
    • Prestegard, J.H.1    Bougault, C.M.2
  • 23
    • 0032517327 scopus 로고    scopus 로고
    • Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses [15]
    • DOI 10.1021/ja982592f
    • Clore GM, Starich MR et al. (1998) Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses. J Am Chem Soc 120: 10571-10572 (Pubitemid 28500376)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.40 , pp. 10571-10572
    • Clore, G.M.1    Starich, M.R.2    Gronenborn, A.M.3
  • 24
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • DOI 10.1021/ja017875d
    • Chou JJ, Kaufman JD et al (2002) Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J Am Chem Soc 124(11): 2450-2451 (Pubitemid 34251754)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.11 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 25
    • 0034755357 scopus 로고    scopus 로고
    • Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel
    • DOI 10.1023/A:1012417721455
    • Ishii Y, Markus MA et al (2001) Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel. J Biomol NMR 21(2): 141-151 (Pubitemid 33040162)
    • (2001) Journal of Biomolecular NMR , vol.21 , Issue.2 , pp. 141-151
    • Ishii, Y.1    Markus, M.A.2    Tycko, R.3
  • 26
    • 45149147257 scopus 로고    scopus 로고
    • Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins
    • DOI 10.1021/ja801729f
    • Lorieau J, Yao L et al (2008) Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins. J Am Chem Soc 130(24): 7536-7537 (Pubitemid 351842104)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.24 , pp. 7536-7537
    • Lorieau, J.1    Yao, L.2    Bax, A.3
  • 28
    • 0033569503 scopus 로고    scopus 로고
    • Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex
    • DOI 10.1006/jmbi.1999.3133
    • Bolon PJ, Al-Hashimi HM et al (1999) Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex. J Mol Biol 293(1): 107-115 (Pubitemid 29494873)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.1 , pp. 107-115
    • Bolon, P.J.1    Al-Hashimi, H.M.2    Prestegard, J.H.3
  • 29
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • DOI 10.1016/0076-6879(89)77007-5
    • Kosen PA (1989) Spin labeling of proteins. Meth Enzymol 177: 86-121 (Pubitemid 20041572)
    • (1989) Methods in Enzymology , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 30
    • 24944497258 scopus 로고    scopus 로고
    • NMR spectroscopy of paramagnetic metalloproteins
    • DOI 10.1002/cbic.200500124
    • Bertini I, Luchinat C et al (2005) NMR spectroscopy of paramagnetic metalloproteins. Chembiochem 6(9): 1536-1549 (Pubitemid 41308942)
    • (2005) ChemBioChem , vol.6 , Issue.9 , pp. 1536-1549
    • Bertini, I.1    Luchinat, C.2    Parigi, G.3    Pierattelli, R.4
  • 31
    • 48749105838 scopus 로고    scopus 로고
    • Prospects for lanthanides in structural biology by NMR
    • Otting G (2008) Prospects for lanthanides in structural biology by NMR. J Biomol NMR 42(1): 1-9
    • (2008) J Biomol NMR , vol.42 , Issue.1 , pp. 1-9
    • Otting, G.1
  • 32
    • 0034674922 scopus 로고    scopus 로고
    • Binding orientation of proline-rich peptides in solution: Polarity of the profilin-ligand interaction
    • Mahoney NM, Rastogi VK et al. (2000) Binding orientation of proline-rich peptides in solution: polarity of the profilin-ligand interaction. J Am Chem Soc 122: 7851-7852
    • (2000) J Am Chem Soc , vol.122 , pp. 7851-7852
    • Mahoney, N.M.1    Rastogi, V.K.2
  • 33
    • 0042033050 scopus 로고
    • Proton relaxation times in paramagnetic solutions. Effects of electron spin relaxation
    • Bloembergen N, Morgan LO (1961) Proton relaxation times in paramagnetic solutions. Effects of electron spin relaxation. J Chem Phys 34: 842-850
    • (1961) J Chem Phys , vol.34 , pp. 842-850
    • Bloembergen, N.1    Morgan, L.O.2
  • 34
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • DOI 10.1021/bi000060h
    • Battiste JL, Wagner G (2000) Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data. Biochemistry 39(18): 5355-5365 (Pubitemid 30257075)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 35
    • 0037533875 scopus 로고    scopus 로고
    • EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement
    • DOI 10.1021/ja034488q
    • Iwahara J, Anderson DE et al (2003) EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement. J Am Chem Soc 125(22): 6634-6635 (Pubitemid 36667439)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.22 , pp. 6634-6635
    • Iwahara, J.1    Anderson, D.E.2    Murphy, E.C.3    Clore, G.M.4
  • 36
    • 33846561471 scopus 로고    scopus 로고
    • 1H transverse paramagnetic relaxation enhancement measurements on macromolecules
    • DOI 10.1016/j.jmr.2006.10.003, PII S109078070600334X
    • Iwahara J, Tang C et al (2007) Practical aspects of (1)H transverse paramagnetic relaxation enhancement measurements on macromolecules. J Magn Reson 184(2): 185-195 (Pubitemid 46177665)
    • (2007) Journal of Magnetic Resonance , vol.184 , Issue.2 , pp. 185-195
    • Iwahara, J.1    Tang, C.2    Marius Clore, G.3
  • 37
    • 35548943472 scopus 로고    scopus 로고
    • Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement
    • DOI 10.1016/j.sbi.2007.08.013, PII S0959440X07001200, Carbohydrates and glycoconjugates / Biophysical methods
    • Clore GM, Tang C et al (2007) Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement. Curr Opin Struct Biol 17(5): 603-616 (Pubitemid 350019011)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.5 , pp. 603-616
    • Clore, G.M.1    Tang, C.2    Iwahara, J.3
  • 38
    • 2442433447 scopus 로고    scopus 로고
    • 1H Paramagnetic Relaxation Enhancement Data Arising from a Flexible Paramagnetic Group Attached to a Macromolecule
    • DOI 10.1021/ja031580d
    • Iwahara J, Schwieters CD et al (2004) Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule. J Am Chem Soc 126(18): 5879-5896 (Pubitemid 38621427)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.18 , pp. 5879-5896
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 39
    • 78049389864 scopus 로고    scopus 로고
    • Integrin beta3 phosphorylation dictates its complex with Shc PTB domain
    • Deshmukh L, Gorbatyuk V et al (2010) Integrin beta3 phosphorylation dictates its complex with Shc PTB domain. J Biol Chem 285: 34875-34884
    • (2010) J Biol Chem , vol.285 , pp. 34875-34884
    • Deshmukh, L.1    Gorbatyuk, V.2
  • 40
    • 51049098984 scopus 로고    scopus 로고
    • The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly
    • Wang X, Fukuda K et al (2008) The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly. J Biol Chem 283 (30): 21113-21119
    • (2008) J Biol Chem , vol.283 , Issue.30 , pp. 21113-21119
    • Wang, X.1    Fukuda, K.2
  • 41
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • Iwahara J, Clore GM (2006) Detecting transient intermediates in macromolecular binding by paramagnetic NMR. Nature 440(7088): 1227-1230
    • (2006) Nature , vol.440 , Issue.7088 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 42
    • 33751086423 scopus 로고    scopus 로고
    • Visualization of transient encounter complexes in protein-protein association
    • DOI 10.1038/nature05201, PII NATURE05201
    • Tang C, Iwahara J et al (2006) Visualization of transient encounter complexes in proteinprotein association. Nature 444(7117): 383-386 (Pubitemid 44764115)
    • (2006) Nature , vol.444 , Issue.7117 , pp. 383-386
    • Tang, C.1    Iwahara, J.2    Clore, G.M.3
  • 43
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes
    • Clore GM, Iwahara J (2009) Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem Rev 109(9): 4108-4139
    • (2009) Chem Rev , vol.109 , Issue.9 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2
  • 46
    • 0032520957 scopus 로고    scopus 로고
    • The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics
    • Ubbink M, Ejdeback M et al (1998) The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics. Structure 6(3): 323-335 (Pubitemid 28159315)
    • (1998) Structure , vol.6 , Issue.3 , pp. 323-335
    • Ubbink, M.1    Ejdeback, M.2    Karlsson, B.G.3    Bendall, D.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.