메뉴 건너뛰기




Volumn 51, Issue 3, 2011, Pages 253-263

Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains

Author keywords

Calmodulin; Conformational heterogeneity; Maximum allowed probability; Maximum occurrence; Paramagnetic proteins; Paramagnetic tag

Indexed keywords

CALMODULIN; LANTHANIDE; PROTEIN;

EID: 80755176789     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-011-9532-2     Document Type: Article
Times cited : (39)

References (52)
  • 1
    • 0037450635 scopus 로고    scopus 로고
    • Structural basis for endothelial nitric oxide synthase binding to calmodulin
    • DOI 10.1093/emboj/cdg078
    • M Aoyagi AS Arvai JA Tainer ED Getzoff 2003 Structural basis for endothelial nitric oxide synthase binding to calmodulin EMBO J 22 766 775 10.1093/emboj/cdg078 (Pubitemid 36227779)
    • (2003) EMBO Journal , vol.22 , Issue.4 , pp. 766-775
    • Aoyagi, M.1    Arvai, A.S.2    Tainer, J.A.3    Getzoff, E.D.4
  • 2
    • 0038101545 scopus 로고    scopus 로고
    • 1H residual dipolar coupling analysis of native and alkaline-K79A Saccharomyces cerevisiae cytochrome c
    • M Assfalg I Bertini P Turano AG Mauk JR Winkler BH Gray 2003 15 N-1H residual dipolar coupling analysis of native and alkaline-K79A S. cerevisiae cytochrome c Biophys J 84 3917 3923 10.1016/S0006-3495(03)75119-4 (Pubitemid 36637886)
    • (2003) Biophysical Journal , vol.84 , Issue.6 , pp. 3917-3923
    • Assfalg, M.1    Bertini, I.2    Turano, P.3    Mauk, A.G.4    Winkler, J.R.5    Gray, H.B.6
  • 3
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • DOI 10.1016/0022-2836(88)90608-0
    • YS Babu CE Bugg WJ Cook 1988 Structure of calmodulin refined at 2.2 Å resolution J Mol Biol 204 191 204 10.1016/0022-2836(88)90608-0 (Pubitemid 19011741)
    • (1988) Journal of Molecular Biology , vol.204 , Issue.1 , pp. 191-204
    • Sudhakar Babu, Y.1    Bugg, C.E.2    Cook, W.J.3
  • 5
    • 3242861343 scopus 로고    scopus 로고
    • The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyano-cytochrome c as an example
    • L Banci I Bertini KL Bren MA Cremonini HB Gray C Luchinat P Turano 1996 The use of pseudo contact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyano-cytochrome c as an example J Biol Inorg Chem 1 117 126 10.1007/s007750050030 (Pubitemid 126510317)
    • (1996) Journal of Biological Inorganic Chemistry , vol.1 , Issue.2 , pp. 117-126
    • Banci, L.1    Bertini, I.2    Bren, K.L.3    Cremonini, M.A.4    Gray, H.B.5    Luchinat, C.6    Turano, P.7
  • 7
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy; The central helix is flexible
    • 10.1021/bi00138a005
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy; the central helix is flexible Biochemistry 31 5269 5278 10.1021/bi00138a005
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 8
    • 74849106907 scopus 로고    scopus 로고
    • Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase
    • 10.1021/ja9064574
    • Q Bashir AN Volkov GM Ullmann M Ubbink 2010 Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase J Am Chem Soc 132 241 247 10.1021/ja9064574
    • (2010) J Am Chem Soc , vol.132 , pp. 241-247
    • Bashir, Q.1    Volkov, A.N.2    Ullmann, G.M.3    Ubbink, M.4
  • 9
    • 0026158667 scopus 로고
    • An efficient 3D NMR technique for correlating the proton and 15 N backbone amide resonances with the alpha-carbon of the preceding residue
    • 10.1007/BF01874573
    • A Bax M Ikura 1991 An efficient 3D NMR technique for correlating the proton and 15 N backbone amide resonances with the alpha-carbon of the preceding residue J Biomol NMR 1 99 104 10.1007/BF01874573
    • (1991) J Biomol NMR , vol.1 , pp. 99-104
    • Bax, A.1    Ikura, M.2
  • 11
    • 0038188962 scopus 로고    scopus 로고
    • Paramagnetic constraints: An aid for quick solution structure determination of paramagnetic metalloproteins
    • 10.1002/cmr.10027
    • I Bertini C Luchinat G Parigi 2002 Paramagnetic constraints: an aid for quick solution structure determination of paramagnetic metalloproteins Concepts Magn Reson 14 259 286 10.1002/cmr.10027
    • (2002) Concepts Magn Reson , vol.14 , pp. 259-286
    • Bertini, I.1    Luchinat, C.2    Parigi, G.3
  • 12
    • 0038723707 scopus 로고    scopus 로고
    • Tuning the affinity for lanthanides of calcium binding proteins
    • DOI 10.1021/bi034494z
    • I Bertini I Gelis N Katsaros C Luchinat A Provenzani 2003 Tuning the affinity for lanthanides of calcium binding proteins Biochemistry 42 8011 8021 10.1021/bi034494z (Pubitemid 36807718)
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 8011-8021
    • Bertini, I.1    Gelis, I.2    Katsaros, N.3    Luchinat, C.4    Provenzani, A.5
  • 14
    • 35548988910 scopus 로고    scopus 로고
    • Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains
    • DOI 10.1021/ja0726613
    • I Bertini YK Gupta C Luchinat G Parigi M Peana L Sgheri J Yuan 2007 Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains J Am Chem Soc 129 12786 12794 10.1021/ja0726613 (Pubitemid 350004491)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.42 , pp. 12786-12794
    • Bertini, I.1    Gupta, Y.K.2    Luchinat, C.3    Parigi, G.4    Peana, M.5    Sgheri, L.6    Yuan, J.7
  • 15
    • 48249097226 scopus 로고    scopus 로고
    • Perspectives in NMR of paramagnetic proteins
    • 10.1039/b719526e
    • I Bertini C Luchinat G Parigi R Pierattelli 2008 Perspectives in NMR of paramagnetic proteins Dalton Trans 2008 3782 3790 10.1039/b719526e
    • (2008) Dalton Trans , vol.2008 , pp. 3782-3790
    • Bertini, I.1    Luchinat, C.2    Parigi, G.3    Pierattelli, R.4
  • 16
    • 67849117178 scopus 로고    scopus 로고
    • Accurate solution structures of proteins from X-ray data and minimal set of NMR data: Calmodulin peptide complexes as examples
    • 10.1021/ja8080764
    • I Bertini P Kursula C Luchinat G Parigi J Vahokoski M Willmans J Yuan 2009 Accurate solution structures of proteins from X-ray data and minimal set of NMR data: calmodulin peptide complexes as examples J Am Chem Soc 131 5134 5144 10.1021/ja8080764
    • (2009) J Am Chem Soc , vol.131 , pp. 5134-5144
    • Bertini, I.1    Kursula, P.2    Luchinat, C.3    Parigi, G.4    Vahokoski, J.5    Willmans, M.6    Yuan, J.7
  • 18
    • 74949117361 scopus 로고    scopus 로고
    • Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion
    • 10.1021/ja909052h
    • JH Cho N O'Connell DP Raleigh AG Palmer III 2010 Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion J Am Chem Soc 132 450 451 10.1021/ja909052h
    • (2010) J Am Chem Soc , vol.132 , pp. 450-451
    • Cho, J.H.1    O'Connell, N.2    Raleigh, D.P.3    Palmer Iii, A.G.4
  • 19
    • 0034753415 scopus 로고    scopus 로고
    • 2+-calmodulin reveals flexible hand-like properties of its domains
    • DOI 10.1038/nsb1101-990
    • 2+ calmodulin reveals flexible hand-like properties of its domains Nature Struct Biol 8 990 997 10.1038/nsb1101-990 (Pubitemid 33032370)
    • (2001) Nature Structural Biology , vol.8 , Issue.11 , pp. 990-997
    • Chou, J.J.1    Li, S.2    Klee, C.B.3    Bax, A.4
  • 20
    • 33846505918 scopus 로고    scopus 로고
    • 3+ ions: Application to the N-terminal domain of cardiac troponin C
    • DOI 10.1007/s10858-006-9105-y
    • 3+ ions: application to the N-terminal domain of cardiac troponin C J Biomol NMR 37 79 95 10.1007/s10858-006-9105-y (Pubitemid 46157974)
    • (2007) Journal of Biomolecular NMR , vol.37 , Issue.2 , pp. 79-95
    • Eichmuller, C.1    Skrynnikov, N.R.2
  • 21
    • 0141594755 scopus 로고    scopus 로고
    • 2+-calmodulin
    • DOI 10.1016/j.str.2003.09.004
    • 2+-calmodulin Structure 11 1303 1307 10.1016/j.str.2003.09.004 (Pubitemid 37214891)
    • (2003) Structure , vol.11 , Issue.10 , pp. 1303-1307
    • Fallon, J.L.1    Quiocho, F.A.2
  • 23
    • 33846230547 scopus 로고    scopus 로고
    • "Four-dimensional" protein structures: Examples from metalloproteins
    • 10.1021/ar050103s
    • M Fragai C Luchinat G Parigi 2006 "Four-dimensional" protein structures: examples from metalloproteins Acc Chem Res 39 909 917 10.1021/ar050103s
    • (2006) Acc Chem Res , vol.39 , pp. 909-917
    • Fragai, M.1    Luchinat, C.2    Parigi, G.3
  • 24
    • 77955809772 scopus 로고    scopus 로고
    • Validation of a lanthanide tag for the analysis of protein dynamics by paramagnetic NMR spectroscopy
    • 10.1021/ja909508r
    • MAS Hass PHJ Keizers A Blok Y Hiruma M Ubbink 2010 Validation of a lanthanide tag for the analysis of protein dynamics by paramagnetic NMR spectroscopy J Am Chem Soc 132 9952 9953 10.1021/ja909508r
    • (2010) J Am Chem Soc , vol.132 , pp. 9952-9953
    • Hass, M.A.S.1    Keizers, P.H.J.2    Blok, A.3    Hiruma, Y.4    Ubbink, M.5
  • 25
    • 70350066141 scopus 로고    scopus 로고
    • DOTA-M8: An extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy
    • 10.1021/ja903233w
    • D Häussinger J Huang S Grzesiek 2009 DOTA-M8: an extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy J Am Chem Soc 131 14761 14767 10.1021/ja903233w
    • (2009) J Am Chem Soc , vol.131 , pp. 14761-14767
    • Häussinger, D.1    Huang, J.2    Grzesiek, S.3
  • 26
    • 27744480205 scopus 로고    scopus 로고
    • Structural biology: Proteins flex to function
    • DOI 10.1038/438036a, PII 438036
    • YJ Huang GT Montelione 2005 Structural biology: proteins flex to function Nature 438 36 37 2005Natur.438...36H 10.1038/438036a (Pubitemid 41599809)
    • (2005) Nature , vol.438 , Issue.7064 , pp. 36-37
    • Huang, Y.J.1    Montelione, G.T.2
  • 27
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • 2006Natur.440.1227I 10.1038/nature04673
    • J Iwahara GM Clore 2006 Detecting transient intermediates in macromolecular binding by paramagnetic NMR Nature 440 1227 1230 2006Natur.440.1227I 10.1038/nature04673
    • (2006) Nature , vol.440 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 28
    • 14844361989 scopus 로고    scopus 로고
    • NMR studies of protein structure and dynamics
    • DOI 10.1016/j.jmr.2004.11.021, PII S1090780704003854
    • LE Kay 2005 NMR studies of protein structure and dynamics J Magn Reson 173 193 207 2005JMagR.173..193K 10.1016/j.jmr.2004.11.021 (Pubitemid 40352443)
    • (2005) Journal of Magnetic Resonance , vol.173 , Issue.2 , pp. 193-207
    • Kay, L.E.1
  • 29
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • LE Kay M Ikura R Tschudin A Bax 1990 Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins J Magn Reson 89 496 514
    • (1990) J Magn Reson , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 30
    • 34547657260 scopus 로고    scopus 로고
    • Increased paramagnetic effect of a lanthanide protein probe by two-point attachment
    • DOI 10.1021/ja0725201
    • PH Keizers JF Desreux M Overhand M Ubbink 2007 Increased paramagnetic effect of a lanthanide protein probe by two-point attachment J Am Chem Soc 129 9292 9293 10.1021/ja0725201 (Pubitemid 47218791)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.30 , pp. 9292-9293
    • Keizers, P.H.J.1    Desreux, J.F.2    Overhand, M.3    Ubbink, M.4
  • 31
    • 55549133637 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment
    • 10.1021/ja8054832
    • PHJ Keizers A Saragliadis Y Hiruma M Overhand M Ubbink 2008 Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment J Am Chem Soc 130 14802 14812 10.1021/ja8054832
    • (2008) J Am Chem Soc , vol.130 , pp. 14802-14812
    • Keizers, P.H.J.1    Saragliadis, A.2    Hiruma, Y.3    Overhand, M.4    Ubbink, M.5
  • 32
    • 77956501272 scopus 로고    scopus 로고
    • A transient and low-populated protein-folding intermediate at atomic resolution
    • 2010Sci.329.1312K 10.1126/science.1191723
    • DM Korzhnev TL Religa W Banachewicz AR Fersht LE Kay 2010 A transient and low-populated protein-folding intermediate at atomic resolution Science 329 1312 1316 2010Sci...329.1312K 10.1126/science.1191723
    • (2010) Science , vol.329 , pp. 1312-1316
    • Korzhnev, D.M.1    Religa, T.L.2    Banachewicz, W.3    Fersht, A.R.4    Kay, L.E.5
  • 34
    • 33746283923 scopus 로고    scopus 로고
    • Efficient determination of the most favoured orientations of protein domains from paramagnetic NMR data
    • DOI 10.1088/0266-5611/22/4/019, PII S0266561106215119, 019
    • M Longinetti C Luchinat G Parigi L Sgheri 2006 Efficient determination of the most favored orientations of protein domains from paramagnetic NMR data Inv Probl 22 1485 1502 2249474 2006InvPr..22.1485L 1095.92033 10.1088/0266-5611/22/ 4/019 (Pubitemid 44102189)
    • (2006) Inverse Problems , vol.22 , Issue.4 , pp. 1485-1502
    • Longinetti, M.1    Luchinat, C.2    Parigi, G.3    Sgheri, L.4
  • 35
    • 0037195266 scopus 로고    scopus 로고
    • Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR
    • DOI 10.1021/bi0264162
    • TK Mal NR Skrynnikov KL Yap LE Kay M Ikura 2002 Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR Biochemistry 41 12899 12906 10.1021/bi0264162 (Pubitemid 35215771)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 12899-12906
    • Mal, T.K.1    Skrynnikov, N.R.2    Yap, K.L.3    Kay, L.E.4    Ikura, M.5
  • 36
    • 33749246223 scopus 로고    scopus 로고
    • Complex of Calmodulin with a Ryanodine Receptor Target Reveals a Novel, Flexible Binding Mode
    • DOI 10.1016/j.str.2006.08.011, PII S0969212606003613
    • AA Maximciuc JA Putkey Y Shamoo KR MacKenzie 2006 Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode Structure 14 1547 1556 10.1016/j.str.2006.08.011 (Pubitemid 44486817)
    • (2006) Structure , vol.14 , Issue.10 , pp. 1547-1556
    • Maximciuc, A.A.1    Putkey, J.A.2    Shamoo, Y.3    MacKenzie, K.R.4
  • 37
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • 1992Sci.257.1251M 10.1126/science.1519061
    • WE Meador AR Means FA Quiocho 1992 Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex Science 257 1251 1255 1992Sci...257.1251M 10.1126/science.1519061
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 38
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • WE Meador AR Means FA Quiocho 1993 Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures Science 262 1718 1721 1993Sci...262.1718M 10.1126/science.8259515 (Pubitemid 24030092)
    • (1993) Science , vol.262 , Issue.5140 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 39
    • 0001689741 scopus 로고
    • Gradient-enhanced triple resonance three-dimensional NMR experiments with improved sensitivity
    • 10.1006/jmrb.1994.1032
    • DR Muhandiram LE Kay 1994 Gradient-enhanced triple resonance three-dimensional NMR experiments with improved sensitivity J Magn Reson Ser B 103 203 216 10.1006/jmrb.1994.1032
    • (1994) J Magn Reson ser B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 40
    • 46949110729 scopus 로고    scopus 로고
    • Numbat: An interactive software tool for fitting Πχ-tensors to molecular coordinates using pseudo contact shifts
    • 10.1007/s10858-008-9249-z
    • C Schmitz MJ Stanton-Cook XC Su G Otting T Huber 2008 Numbat: an interactive software tool for fitting Πχ-tensors to molecular coordinates using pseudo contact shifts J Biomol NMR 41 179 189 10.1007/s10858-008-9249-z
    • (2008) J Biomol NMR , vol.41 , pp. 179-189
    • Schmitz, C.1    Stanton-Cook, M.J.2    Su, X.C.3    Otting, G.4    Huber, T.5
  • 42
    • 78049423923 scopus 로고    scopus 로고
    • Joining RDC data from flexible protein domains
    • 2732913 2010InvPr.26k5021S 10.1088/0266-5611/26/11/115021
    • L Sgheri 2010 Joining RDC data from flexible protein domains Inv Probl 26 12 115021 2732913 2010InvPr..26k5021S 10.1088/0266-5611/26/11/115021
    • (2010) Inv Probl , vol.26 , Issue.12 , pp. 115021
    • Sgheri, L.1
  • 43
    • 77649191190 scopus 로고    scopus 로고
    • Paramagnetic labelling of proteins and oligonucleotides for NMR
    • 10.1007/s10858-009-9331-1
    • XC Su G Otting 2010 Paramagnetic labelling of proteins and oligonucleotides for NMR J Biomol NMR 46 101 112 10.1007/s10858-009-9331-1
    • (2010) J Biomol NMR , vol.46 , pp. 101-112
    • Su, X.C.1    Otting, G.2
  • 44
    • 33749680579 scopus 로고    scopus 로고
    • Site-specific labelling of proteins with a rigid lanthanide-binding tag
    • DOI 10.1002/cbic.200600142
    • XC Su T Huber NE Dixon G Otting 2006 Site-specific labelling of proteins with a rigid lanthanide-binding tag Chem Bio Chem 7 1599 1604 (Pubitemid 44556007)
    • (2006) ChemBioChem , vol.7 , Issue.10 , pp. 1599-1604
    • Su, X.-C.1    Huber, T.2    Dixon, N.E.3    Otting, G.4
  • 46
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • DOI 10.1038/nature06232, PII NATURE06232
    • C Tang CD Schwieters GM Clore 2007 Open-to-close transition in apo maltose-binding protein observed by paramagnetic NMR Nature 449 1078 1082 2007Natur.449.1078T 10.1038/nature06232 (Pubitemid 350014601)
    • (2007) Nature , vol.449 , Issue.7165 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 47
    • 50149085281 scopus 로고    scopus 로고
    • Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
    • 2008PNAS.10511766V 10.1073/pnas.0804221105
    • P Vallurupalli DF Hansen LE Kay 2008 Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy Proc Natl Acad Sci USA 105 11766 11771 2008PNAS..10511766V 10.1073/pnas.0804221105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11766-11771
    • Vallurupalli, P.1    Hansen, D.F.2    Kay, L.E.3
  • 48
    • 37549050579 scopus 로고    scopus 로고
    • Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR
    • 10.1016/j.jmb.2007.11.056
    • MD Vlasie R Fernández-Busnadiego M Prudêncio M Ubbink 2008 Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR J Mol Biol 375 1405 1415 10.1016/j.jmb.2007.11.056
    • (2008) J Mol Biol , vol.375 , pp. 1405-1415
    • Vlasie, M.D.1    Fernández-Busnadiego, R.2    Prudêncio, M.3    Ubbink, M.4
  • 52
    • 46449126204 scopus 로고    scopus 로고
    • Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints
    • DOI 10.1110/ps.034561.108
    • T Zhuang HS Lee B Imperiali JH Prestegard 2008 Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints Protein Sci 17 1220 1231 10.1110/ps.034561.108 (Pubitemid 351930919)
    • (2008) Protein Science , vol.17 , Issue.7 , pp. 1220-1231
    • Zhuang, T.1    Lee, H.-S.2    Imperiali, B.3    Prestegard, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.