메뉴 건너뛰기




Volumn 55, Issue 2, 2013, Pages 157-166

A systematic study of labelling an α-helix in a protein with a lanthanide using IDA-SH or NTA-SH tags

Author keywords

ERp29; IDA SH tag; Lanthanide tag; NMR spectroscopy; NTA SH tag; Pseudocontact shifts

Indexed keywords

ASPARTIC ACID; CYSTEINE; DIGLYCINE; GLUTAMIC ACID; LANTHANIDE; MUTANT PROTEIN; NITRILOTRIACETIC ACID;

EID: 84878853949     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-012-9697-3     Document Type: Article
Times cited : (25)

References (49)
  • 1
    • 0034600246 scopus 로고    scopus 로고
    • Lanthanide-induced pseudocontact shifts for solution structure refinements of macromolecules in shells up to 40 Å from the metal ion
    • 10.1021/ja993691b
    • Allegrozzi M, Bertini I, Janik MBL, Lee YM, Liu G, Luchinat C (2000) Lanthanide-induced pseudocontact shifts for solution structure refinements of macromolecules in shells up to 40 Å from the metal ion. J Am Chem Soc 122:4154-4161
    • (2000) J Am Chem Soc , vol.122 , pp. 4154-4161
    • Allegrozzi, M.1    Bertini, I.2    Janik, M.B.L.3    Lee, Y.M.4    Liu, G.5    Luchinat, C.6
  • 6
    • 81855172065 scopus 로고    scopus 로고
    • Binding of low-molecular weight inhibitors promotes large conformational changes in the dengue virus NS2B-NS3 protease: Fold analysis by pseudocontact shifts
    • 10.1021/ja208435s
    • de la Cruz L, Nguyen THD, Ozawa K, Shin J, Graham B, Huber T, Otting G (2011) Binding of low-molecular weight inhibitors promotes large conformational changes in the dengue virus NS2B-NS3 protease: fold analysis by pseudocontact shifts. J Am Chem Soc 133:19205-19215
    • (2011) J Am Chem Soc , vol.133 , pp. 19205-19215
    • De La Cruz, L.1    Nguyen, T.H.D.2    Ozawa, K.3    Shin, J.4    Graham, B.5    Huber, T.6    Otting, G.7
  • 8
    • 0037174538 scopus 로고    scopus 로고
    • Derivation of structural restraints using a thiol-reactive chelator
    • 10.1016/S0014-5793(02)03297-0
    • Dvoretsky A, Gaponenko V, Rosevear PR (2002) Derivation of structural restraints using a thiol-reactive chelator. FEBS Lett 528:189-192
    • (2002) FEBS Lett , vol.528 , pp. 189-192
    • Dvoretsky, A.1    Gaponenko, V.2    Rosevear, P.R.3
  • 10
    • 70350066141 scopus 로고    scopus 로고
    • DOTA-M8: An extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy
    • 10.1021/ja903233w
    • Häussinger D, Huang J, Grzesiek S (2009) DOTA-M8: an extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy. J Am Chem Soc 131:14761-14767
    • (2009) J Am Chem Soc , vol.131 , pp. 14761-14767
    • Häussinger, D.1    Huang, J.2    Grzesiek, S.3
  • 11
    • 3042724646 scopus 로고    scopus 로고
    • Novel techniques for weak alignment of proteins in solution using chemical tags coordinating lanthanide ions
    • 10.1023/B:JNMR.0000032611.72827.de
    • Ikegami T, Verdier L, Sakhaii P, Grimme S, Pescatore B, Saxena K, Fiebig KM, Griesinger C (2004) Novel techniques for weak alignment of proteins in solution using chemical tags coordinating lanthanide ions. J Biomol NMR 29:339-349
    • (2004) J Biomol NMR , vol.29 , pp. 339-349
    • Ikegami, T.1    Verdier, L.2    Sakhaii, P.3    Grimme, S.4    Pescatore, B.5    Saxena, K.6    Fiebig, K.M.7    Griesinger, C.8
  • 12
    • 79957940344 scopus 로고    scopus 로고
    • 4, 4′-dithiobisdipicolinic acid: A small and convenient lanthanide binding tag for protein NMR spectroscopy
    • 10.1002/chem.201003573
    • Jia X, Maleckis A, Huber T, Otting G (2011) 4, 4′- dithiobisdipicolinic acid: a small and convenient lanthanide binding tag for protein NMR spectroscopy. Chem Eur J 17:6830-6836
    • (2011) Chem Eur J , vol.17 , pp. 6830-6836
    • Jia, X.1    Maleckis, A.2    Huber, T.3    Otting, G.4
  • 13
    • 29044440989 scopus 로고    scopus 로고
    • Weak alignment of paramagnetic proteins warrants correction for residual CSA effects in measurements of pseudocontact shifts
    • 10.1021/ja0564259
    • John M, Park AY, Pintacuda G, Dixon NE, Otting G (2005) Weak alignment of paramagnetic proteins warrants correction for residual CSA effects in measurements of pseudocontact shifts. J Am Chem Soc 127:17190-17191
    • (2005) J Am Chem Soc , vol.127 , pp. 17190-17191
    • John, M.1    Park, A.Y.2    Pintacuda, G.3    Dixon, N.E.4    Otting, G.5
  • 14
    • 33749504901 scopus 로고    scopus 로고
    • Structure determination of protein-ligand complexes by transferred paramagnetic shifts
    • 10.1021/ja063584z
    • John M, Pintacuda G, Park AY, Dixon NE, Otting G (2006) Structure determination of protein-ligand complexes by transferred paramagnetic shifts. J Am Chem Soc 128:12910-12916
    • (2006) J Am Chem Soc , vol.128 , pp. 12910-12916
    • John, M.1    Pintacuda, G.2    Park, A.Y.3    Dixon, N.E.4    Otting, G.5
  • 16
    • 34547657260 scopus 로고    scopus 로고
    • Increased paramagnetic effect of a lanthanide protein probe by two-point attachment
    • 10.1021/ja0725201
    • Keizers PH, Desreux JF, Overhand M, Ubbink M (2007) Increased paramagnetic effect of a lanthanide protein probe by two-point attachment. J Am Chem Soc 129:9292-9293
    • (2007) J Am Chem Soc , vol.129 , pp. 9292-9293
    • Keizers, P.H.1    Desreux, J.F.2    Overhand, M.3    Ubbink, M.4
  • 17
    • 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
    • Keizers PH, Saragliadis A, Hiruma Y, Overhand M, Ubbink M (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
    • (2008) J Am Chem Soc , vol.130 , pp. 14802-14812
    • Keizers, P.H.1    Saragliadis, A.2    Hiruma, Y.3    Overhand, M.4    Ubbink, M.5
  • 20
    • 80054959777 scopus 로고    scopus 로고
    • Expanding the utility of NMR restraints with paramagnetic compounds: Background and practical aspects
    • 10.1016/j.pnmrs.2011.05.001
    • Koehler J, Meiler J (2011) Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects. Prog Nucl Magn Reson Spectr 59:360-389
    • (2011) Prog Nucl Magn Reson Spectr , vol.59 , pp. 360-389
    • Koehler, J.1    Meiler, J.2
  • 21
    • 14944346562 scopus 로고    scopus 로고
    • Residual dipolar coupling constants: An elementary derivation of key equations
    • 10.1002/cmr.a.20003
    • Kramer F, Deshmukh MV, Kessler H, Glaser SJ (2004) Residual dipolar coupling constants: an elementary derivation of key equations. Concepts Magn Reson 21A:10-21
    • (2004) Concepts Magn Reson , vol.21 , pp. 10-21
    • Kramer, F.1    Deshmukh, M.V.2    Kessler, H.3    Glaser, S.J.4
  • 22
    • 84863115471 scopus 로고    scopus 로고
    • Thiol-ene reaction: A versatile tool in site-specific labelling of proteins with chemically inert tags for paramagnetic NMR
    • 10.1039/c2cc17900h
    • Li QF, Yang Y, Maleckis A, Otting G, Su XC (2012) Thiol-ene reaction: a versatile tool in site-specific labelling of proteins with chemically inert tags for paramagnetic NMR. Chem Commun 48:2704-2706
    • (2012) Chem Commun , vol.48 , pp. 2704-2706
    • Li, Q.F.1    Yang, Y.2    Maleckis, A.3    Otting, G.4    Su, X.C.5
  • 23
    • 0034989106 scopus 로고    scopus 로고
    • Thioredoxin-fold as a homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa homodimer
    • 10.1016/S0969-2126(01)00607-4
    • Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S (2001) Thioredoxin-fold as a homodimerization module in the putative chaperone ERp29: nMR structures of the domains and experimental model of the 51 kDa homodimer. Structure 9:457-471
    • (2001) Structure , vol.9 , pp. 457-471
    • Liepinsh, E.1    Baryshev, M.2    Sharipo, A.3    Ingelman-Sundberg, M.4    Otting, G.5    Mkrtchian, S.6
  • 25
    • 0034293196 scopus 로고    scopus 로고
    • Lanthanide ions bind specifically to added "eF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy
    • 2000JMagR.146.381M 10.1006/jmre.2000.2172
    • Ma C, Opella SJ (2000) lanthanide ions bind specifically to added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy. J Magn Reson 146:381-384
    • (2000) J Magn Reson , vol.146 , pp. 381-384
    • Ma, C.1    Opella, S.J.2
  • 26
    • 77949767513 scopus 로고    scopus 로고
    • 3-Mercapto-2, 6-pyridinedicarboxylic acid, a small lanthanide-binding tag for protein studies by NMR spectroscopy
    • 10.1002/chem.200902904
    • Man B, Su XC, Liang H, Simonsen S, Huber T, Messerle B, Otting G (2010) 3-Mercapto-2, 6-pyridinedicarboxylic acid, a small lanthanide-binding tag for protein studies by NMR spectroscopy. Chem Eur J 16:3827-3832
    • (2010) Chem Eur J , vol.16 , pp. 3827-3832
    • Man, B.1    Su, X.C.2    Liang, H.3    Simonsen, S.4    Huber, T.5    Messerle, B.6    Otting, G.7
  • 28
    • 0034601780 scopus 로고    scopus 로고
    • Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: A model derived from DNA-binding studies of mutant proteins by surface plasmon resonance
    • 10.1021/bi001174w
    • Neylon C, Brown SE, Kralicek AV, Miles CS, Love CA, Dixon NE (2000) Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance. Biochemistry 39:11989-11999
    • (2000) Biochemistry , vol.39 , pp. 11989-11999
    • Neylon, C.1    Brown, S.E.2    Kralicek, A.V.3    Miles, C.S.4    Love, C.A.5    Dixon, N.E.6
  • 29
    • 48749105838 scopus 로고    scopus 로고
    • Prospects for lanthanides in structural biology by NMR
    • 10.1007/s10858-008-9256-0
    • Otting G (2008) Prospects for lanthanides in structural biology by NMR. J Biomol NMR 42:1-9
    • (2008) J Biomol NMR , vol.42 , pp. 1-9
    • Otting, G.1
  • 30
    • 77952915958 scopus 로고    scopus 로고
    • Protein NMR using paramagnetic ions
    • 10.1146/annurev.biophys.093008.131321
    • Otting G (2010) Protein NMR using paramagnetic ions. Annu Rev Biophys 39:387-405
    • (2010) Annu Rev Biophys , vol.39 , pp. 387-405
    • Otting, G.1
  • 32
    • 33645390370 scopus 로고    scopus 로고
    • Lanthanide labeling offers fast NMR approach to 3D structure determination of protein-protein complexes
    • 10.1021/ja057008z
    • Pintacuda G, Park AY, Keniry MA, Dixon NE, Otting G (2006) Lanthanide labeling offers fast NMR approach to 3D structure determination of protein-protein complexes. J Am Chem Soc 128:3696-3702
    • (2006) J Am Chem Soc , vol.128 , pp. 3696-3702
    • Pintacuda, G.1    Park, A.Y.2    Keniry, M.A.3    Dixon, N.E.4    Otting, G.5
  • 33
    • 34147204158 scopus 로고    scopus 로고
    • NMR structure determination of protein-ligand complexes by lanthanide labelling
    • 10.1021/ar050087z
    • Pintacuda G, John M, Su XC, Otting G (2007) NMR structure determination of protein-ligand complexes by lanthanide labelling. Acc Chem Res 40:206-212
    • (2007) Acc Chem Res , vol.40 , pp. 206-212
    • Pintacuda, G.1    John, M.2    Su, X.C.3    Otting, G.4
  • 36
    • 67649408735 scopus 로고    scopus 로고
    • Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect
    • 10.1007/s10858-009-9325-z
    • Saio T, Ogura K, Yokochi M, Kobashigawa Y, Inagaki F (2009) Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect. J Biomol NMR 44:157-166
    • (2009) J Biomol NMR , vol.44 , pp. 157-166
    • Saio, T.1    Ogura, K.2    Yokochi, M.3    Kobashigawa, Y.4    Inagaki, F.5
  • 37
    • 77951683740 scopus 로고    scopus 로고
    • PCS-based structure determination of protein-protein complexes
    • 10.1007/s10858-010-9401-4
    • Saio T, Yokochi M, Kumeta H, Inagaki F (2010) PCS-based structure determination of protein-protein complexes. J Biomol NMR 46:271-280
    • (2010) J Biomol NMR , vol.46 , pp. 271-280
    • Saio, T.1    Yokochi, M.2    Kumeta, H.3    Inagaki, F.4
  • 38
    • 80755153749 scopus 로고    scopus 로고
    • An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe
    • 10.1007/s10858-011-9566-5
    • Saio T, Ogura K, Shimizu K, Yokochi M, Burke TR Jr, Inagaki F (2011) An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe. J Biomol NMR 51:395-408
    • (2011) J Biomol NMR , vol.51 , pp. 395-408
    • Saio, T.1    Ogura, K.2    Shimizu, K.3    Yokochi, M.4    Burke, Jr.T.R.5    Inagaki, F.6
  • 39
    • 33745634632 scopus 로고    scopus 로고
    • Efficient χ-tensor determination and NH assignment of paramagnetic proteins
    • 10.1007/s10858-006-9002-4
    • Schmitz C, Park AY, Dixon NE, Otting G, Pintacuda G, Huber T (2006) Efficient χ-tensor determination and NH assignment of paramagnetic proteins. J Biomol NMR 35:79-87
    • (2006) J Biomol NMR , vol.35 , pp. 79-87
    • Schmitz, C.1    Park, A.Y.2    Dixon, N.E.3    Otting, G.4    Pintacuda, G.5    Huber, T.6
  • 40
    • 46949110729 scopus 로고    scopus 로고
    • Numbat: An interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts
    • 10.1007/s10858-008-9249-z
    • Schmitz C, Stanton-Cook MJ, Su XC, Otting G, Huber T (2008) Numbat: an interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts. J Biomol NMR 41:179-189
    • (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
  • 41
    • 84857636811 scopus 로고    scopus 로고
    • Protein structure determination from pseudocontact shifts using ROSETTA
    • 10.1016/j.jmb.2011.12.056
    • Schmitz C, Vernon R, Otting G, Baker D, Huber T (2012) Protein structure determination from pseudocontact shifts using ROSETTA. J Mol Biol 416:668-677
    • (2012) J Mol Biol , vol.416 , pp. 668-677
    • Schmitz, C.1    Vernon, R.2    Otting, G.3    Baker, D.4    Huber, T.5
  • 42
    • 77649191190 scopus 로고    scopus 로고
    • Paramagnetic labelling of proteins and oligonucleotides for NMR
    • 10.1007/s10858-009-9331-1
    • Su XC, Otting G (2010) Paramagnetic labelling of proteins and oligonucleotides for NMR. J Biomol NMR 46:101-112
    • (2010) J Biomol NMR , vol.46 , pp. 101-112
    • Su, X.C.1    Otting, G.2
  • 43
    • 33749680579 scopus 로고    scopus 로고
    • Site-specific labelling of proteins with a rigid lanthanide-binding tag
    • Su XC, Huber T, Dixon NE, Otting G (2006) Site-specific labelling of proteins with a rigid lanthanide-binding tag. Chem BioChem 7:1599-1604
    • (2006) Chem BioChem , vol.7 , pp. 1599-1604
    • Su, X.C.1    Huber, T.2    Dixon, N.E.3    Otting, G.4
  • 45
    • 68049094207 scopus 로고    scopus 로고
    • 3- is a convenient paramagnetic shift reagent for protein NMR studies
    • 10.1021/ja9034957
    • 3- is a convenient paramagnetic shift reagent for protein NMR studies. J Am Chem Soc 131:10352-10353
    • (2009) J Am Chem Soc , vol.131 , pp. 10352-10353
    • Su, X.C.1    Liang, H.2    Loscha, K.V.3    Otting, G.4
  • 46
    • 79955490254 scopus 로고    scopus 로고
    • An iminodiacetic acid based lanthanide binding tag for paramagnetic exchange NMR spectroscopy
    • 10.1002/anie.201007221
    • Swarbrick JD, Ung P, Chhabra S, Graham B (2011a) An iminodiacetic acid based lanthanide binding tag for paramagnetic exchange NMR spectroscopy. Angew Chem Int Ed 50:4403-4406
    • (2011) Angew Chem Int Ed , vol.50 , pp. 4403-4406
    • Swarbrick, J.D.1    Ung, P.2    Chhabra, S.3    Graham, B.4
  • 47
    • 79959383052 scopus 로고    scopus 로고
    • Engineering of a bis-chelator motif into a protein α-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy
    • 10.1039/c1cc11893e
    • Swarbrick JD, Ung P, Su XC, Maleckis A, Chhabra S, Huber T, Otting G, Graham B (2011b) Engineering of a bis-chelator motif into a protein α-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy. Chem Commun 47:7368-7370
    • (2011) Chem Commun , vol.47 , pp. 7368-7370
    • Swarbrick, J.D.1    Ung, P.2    Su, X.C.3    Maleckis, A.4    Chhabra, S.5    Huber, T.6    Otting, G.7    Graham, B.8
  • 49
    • 0242299265 scopus 로고    scopus 로고
    • Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings
    • 10.1021/ja036022d
    • Wöhnert J, Franz KJ, Nitz M, Imperiali B, Schwalbe H (2003) Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings. J Am Chem Soc 125:13338-13339
    • (2003) J Am Chem Soc , vol.125 , pp. 13338-13339
    • Wöhnert, J.1    Franz, K.J.2    Nitz, M.3    Imperiali, B.4    Schwalbe, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.