메뉴 건너뛰기




Volumn 434, Issue 1, 2011, Pages 37-48

Identification of regions responsible for the open conformation of S100A10 using chimaeric S100A11-S100A10 proteins

Author keywords

Annexin; Calcium binding protein; EF hand; NMR spectroscopy; Phospholipid binding protein; S100A11

Indexed keywords

BIS ANS (4,4' DIANILINO 1,1' BINAPHTHYL 5,5' DISULFONIC ACID,DIPOTASSIUM SALT; CALCIUM BINDING PROTEIN; CHIMERIC PROTEIN; LIPOCORTIN 2; PROTEIN S 100; PROTEIN S 100A10; PROTEIN S 100A11; SEPHAROSE; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79251553734     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100887     Document Type: Article
Times cited : (11)

References (62)
  • 1
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T. and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2, 758-767
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 2
    • 0032462776 scopus 로고    scopus 로고
    • A change-in-hand mechanism for S100 signalling
    • Smith, S. P. and Shaw, G. S. (1998) A change-in-hand mechanism for S100 signalling. Biochem. Cell Biol. 76, 324-333
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 324-333
    • Smith, S.P.1    Shaw, G.S.2
  • 3
    • 0029088936 scopus 로고
    • Structures of the troponin C regulatory domains in the apo and calcium-saturated states
    • Gagne, S. M., Tsuda, S., Li, M. X., Smillie, L. B. and Sykes, B. D. (1995) Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nat. Struct. Biol. 2, 784-789
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 784-789
    • Gagne, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 4
    • 33744782044 scopus 로고    scopus 로고
    • Calcium-dependent and -independent interactions of the S100 protein family
    • DOI 10.1042/BJ20060195
    • Santamaria-Kisiel, L., Rintala-Dempsey, A. C. and Shaw, G. S. (2006) Calcium-dependent and -independent interactions of the S100 protein family. Biochem. J. 396, 201-214 (Pubitemid 43837235)
    • (2006) Biochemical Journal , vol.396 , Issue.2 , pp. 201-214
    • Santamaria-Kisiel, L.1    Rintala-Dempsey, A.C.2    Shaw, G.S.3
  • 5
    • 0034995073 scopus 로고    scopus 로고
    • S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • Donato, R. (2001) S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell Biol. 33, 637-668
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 637-668
    • Donato, R.1
  • 6
    • 0032407132 scopus 로고    scopus 로고
    • Association of S100B with intermediate filaments and microtubules in glial cells
    • Sorci, G., Agneletti, A. L., Bianchi, R. and Donato, R. (1998) Association of S100B with intermediate filaments and microtubules in glial cells. Biochim. Biophys. Acta 1448, 277-289
    • (1998) Biochim. Biophys. Acta , vol.1448 , pp. 277-289
    • Sorci, G.1    Agneletti, A.L.2    Bianchi, R.3    Donato, R.4
  • 8
    • 0027155323 scopus 로고
    • Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart
    • Zeng, F. Y., Gerke, V. and Gabius, H. J. (1993) Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart. Int. J. Biochem. 25, 1019-1027
    • (1993) Int. J. Biochem. , vol.25 , pp. 1019-1027
    • Zeng, F.Y.1    Gerke, V.2    Gabius, H.J.3
  • 10
    • 0028879992 scopus 로고
    • Interaction of calcyclin and its cyanogen bromide fragments with annexin II and glyceraldehyde 3-phosphate dehydrogenase
    • Filipek, A., Wojda, U. and Lesniak, W. (1995) Interaction of calcyclin and its cyanogen bromide fragments with annexin II and glyceraldehyde 3-phosphate dehydrogenase. Int. J. Biochem. Cell Biol. 27, 1123-1131
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 1123-1131
    • Filipek, A.1    Wojda, U.2    Lesniak, W.3
  • 11
    • 53749106126 scopus 로고    scopus 로고
    • Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: A novel mode for S100 protein target recognition
    • Lee, Y. T., Dimitrova, Y. N., Schneider, G., Ridenour, W. B., Bhattacharya, S., Soss, S. E., Caprioli, R. M., Filipek, A. and Chazin, W. J. (2008) Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition. Biochemistry 47, 10921-10932
    • (2008) Biochemistry , vol.47 , pp. 10921-10932
    • Lee, Y.T.1    Dimitrova, Y.N.2    Schneider, G.3    Ridenour, W.B.4    Bhattacharya, S.5    Soss, S.E.6    Caprioli, R.M.7    Filipek, A.8    Chazin, W.J.9
  • 12
    • 0037047290 scopus 로고    scopus 로고
    • CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family
    • Filipek, A., Jastrzebska, B., Nowotny, M. and Kuznicki, J. (2002) CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family. J. Biol. Chem. 277, 28848-28852
    • (2002) J. Biol. Chem. , vol.277 , pp. 28848-28852
    • Filipek, A.1    Jastrzebska, B.2    Nowotny, M.3    Kuznicki, J.4
  • 13
    • 0030849323 scopus 로고    scopus 로고
    • Annexin i targets S100C to early endosomes
    • DOI 10.1016/S0014-5793(97)00911-3, PII S0014579397009113
    • Seemann, J., Weber, K. and Gerke, V. (1997) Annexin I targets S100C to early endosomes. FEBS Lett. 413, 185-190 (Pubitemid 27348661)
    • (1997) FEBS Letters , vol.413 , Issue.1 , pp. 185-190
    • Seemann, J.1    Weber, K.2    Gerke, V.3
  • 14
    • 0029811498 scopus 로고    scopus 로고
    • Structural requirements for annexin I-S100C complex formation
    • Seemann, J., Weber, K. and Gerke, V. (1996) Structural requirements for annexin I-S100C complex formation. Biochem. J. 319, 123-129
    • (1996) Biochem. J. , vol.319 , pp. 123-129
    • Seemann, J.1    Weber, K.2    Gerke, V.3
  • 15
    • 33845406931 scopus 로고    scopus 로고
    • Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2
    • Rintala-Dempsey, A. C., Santamaria-Kisiel, L., Liao, Y., Lajoie, G. and Shaw, G. S. (2006) Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2. Biochemistry 45, 14695-14705
    • (2006) Biochemistry , vol.45 , pp. 14695-14705
    • Rintala-Dempsey, A.C.1    Santamaria-Kisiel, L.2    Liao, Y.3    Lajoie, G.4    Shaw, G.S.5
  • 16
    • 0242272321 scopus 로고    scopus 로고
    • Subcellular localization of S100A11 (S100C) in LLC-PK1 renal cells: Calcium- and protein kinase C-dependent association of S100A11 with S100B and vimentin intermediate filaments
    • Bianchi, R., Giambanco, I., Arcuri, C. and Donato, R. (2003) Subcellular localization of S100A11 (S100C) in LLC-PK1 renal cells: calcium- and protein kinase C-dependent association of S100A11 with S100B and vimentin intermediate filaments. Microsc. Res. Tech. 60, 639-651
    • (2003) Microsc. Res. Tech. , vol.60 , pp. 639-651
    • Bianchi, R.1    Giambanco, I.2    Arcuri, C.3    Donato, R.4
  • 18
    • 0038342516 scopus 로고    scopus 로고
    • Unmasking the annexin I interaction from the structure of Apo-S100A11
    • Dempsey, A. C., Walsh, M. P. and Shaw, G. S. (2003) Unmasking the annexin I interaction from the structure of Apo-S100A11. Structure 11, 887-897
    • (2003) Structure , vol.11 , pp. 887-897
    • Dempsey, A.C.1    Walsh, M.P.2    Shaw, G.S.3
  • 22
    • 36349028713 scopus 로고    scopus 로고
    • S100A10/p11: Family, friends and functions
    • Rescher, U. and Gerke, V. (2008) S100A10/p11: family, friends and functions. Pflügers Arch. 455, 575-582
    • (2008) Pflügers Arch. , vol.455 , pp. 575-582
    • Rescher, U.1    Gerke, V.2
  • 26
    • 33646344655 scopus 로고    scopus 로고
    • Design of a protein kinase-inducible domain
    • Balakrishnan, S. and Zondlo, N. J. (2006) Design of a protein kinase-inducible domain. J. Am. Chem. Soc. 128, 5590-5591
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5590-5591
    • Balakrishnan, S.1    Zondlo, N.J.2
  • 27
    • 0025367420 scopus 로고
    • Calcium binding proteins: Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments. Biochem
    • Marsden, B. J., Shaw, G. S. and Sykes, B. D. (1990) Calcium binding proteins: elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments. Biochem. Cell Biol. 68, 587-601
    • (1990) Cell Biol. , vol.68 , pp. 587-601
    • Marsden, B.J.1    Shaw, G.S.2    Sykes, B.D.3
  • 28
    • 0028173452 scopus 로고
    • A calbindin D(9k) mutant with reduced calcium affinity and enhanced cooperativity. Metal ion binding, stability, and structural studies
    • DOI 10.1021/bi00207a015
    • Linse, S., Bylsma, N. R., Drakenberg, T., Sellers, P., Forsen, S., Thulin, E., Svensson, L. A., Zajtzeva, I., Zajtsev, V. and Marek, J. (1994) A calbindin D9k mutant with reduced calcium affinity and enhanced cooperativity: metal ion binding, stability, and structural studies. Biochemistry 33, 12478-12486 (Pubitemid 24340454)
    • (1994) Biochemistry , vol.33 , Issue.41 , pp. 12478-12486
    • Linse, S.1    Bylsma, N.R.2    Drakenberg, T.3    Sellers, P.4    Forsen, S.5    Thulin, E.6    Svensson, L.A.7    Zajtzeva, I.8    Zajtsev, V.9    Marek, J.10
  • 32
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange Site-Directed Mutagenesis
    • Wang, W. and Malcolm, B. A. (1999) Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange Site-Directed Mutagenesis. Biotechniques 26, 680-682
    • (1999) Biotechniques , vol.26 , pp. 680-682
    • Wang, W.1    Malcolm, B.A.2
  • 35
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P. and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 36
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay, L. E., Ikura, M., Tschudin, R. and Bax, A. (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
  • 37
    • 43949167657 scopus 로고
    • HNCACB, a high sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the α-carbon and β-carbon resonances in proteins
    • Wittekind, M. and Mueller, L. (1993) HNCACB, a high sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the α-carbon and β-carbon resonances in proteins. J. Magn. Reson. B101, 201-205
    • (1993) J. Magn. Reson. , vol.B101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 38
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114, 6291-6293
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 39
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 40
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A. and Belvins, R. A. (1994) NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Belvins, R.A.2
  • 41
    • 79251568687 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 42
    • 0027305754 scopus 로고
    • The solution structures of mutant calbindin D9k's, as determined by NMR, show that the calcium-binding site can adopt different folds
    • Johansson, C., Ullner, M. and Drakenberg, T. (1993) The solution structures of mutant calbindin D9k's, as determined by NMR, show that the calcium-binding site can adopt different folds. Biochemistry 32, 8429-8438
    • (1993) Biochemistry , vol.32 , pp. 8429-8438
    • Johansson, C.1    Ullner, M.2    Drakenberg, T.3
  • 43
    • 0020490704 scopus 로고
    • Physicochemical and optical studies on calcium- and potassium-induced conformational changes in bovine brain S-100b protein
    • Mani, R. S., Boyes, B. E. and Kay, C. M. (1982) Physicochemical and optical studies on calcium- and potassium-induced conformational changes in bovine brain S-100b protein. Biochemistry 21, 2607-2612
    • (1982) Biochemistry , vol.21 , pp. 2607-2612
    • Mani, R.S.1    Boyes, B.E.2    Kay, C.M.3
  • 44
  • 45
    • 0021995912 scopus 로고
    • Rat brain S100b protein: Purification, characterization, and ion binding properties. A comparison with bovine S100b protein
    • Baudier, J., Labourdette, G. and Gerard, D. (1985) Rat brain S100b protein: purification, characterization, and ion binding properties. A comparison with bovine S100b protein. J. Neurochem. 44, 76-84
    • (1985) J. Neurochem. , vol.44 , pp. 76-84
    • Baudier, J.1    Labourdette, G.2    Gerard, D.3
  • 46
    • 0023368482 scopus 로고
    • Fluorescence dynamics studies of troponin C
    • Steiner, R. F. and Norris, L. (1987) Fluorescence dynamics studies of troponin C. Biopolymers 26, 1189-1204
    • (1987) Biopolymers , vol.26 , pp. 1189-1204
    • Steiner, R.F.1    Norris, L.2
  • 47
    • 0019977613 scopus 로고
    • Properties of the complexes formed by 1-anilinonaphthalene-8-sulfonate with phosphorylase kinase and calmodulin
    • Steiner, R. F. and Sternberg, H. (1982) Properties of the complexes formed by 1-anilinonaphthalene-8-sulfonate with phosphorylase kinase and calmodulin. Biopolymers 21, 1411-1425
    • (1982) Biopolymers , vol.21 , pp. 1411-1425
    • Steiner, R.F.1    Sternberg, H.2
  • 48
    • 0026623542 scopus 로고
    • Protein-protein interaction studied by site-directed mutagenesis: Characterization of the annexin II binding site on p11, a member of the S100 protein family
    • Kube, E., Becker, T., Weber, K. and Gerke, V. (1992) Protein-protein interaction studied by site-directed mutagenesis: characterization of the annexin II binding site on p11, a member of the S100 protein family. J. Biol. Chem. 267, 14175-14182
    • (1992) J. Biol. Chem. , vol.267 , pp. 14175-14182
    • Kube, E.1    Becker, T.2    Weber, K.3    Gerke, V.4
  • 49
    • 0025678441 scopus 로고
    • Protein - Protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11
    • Becker, T., Weber, K. and Johnsson, N. (1990) Protein-protein recognition via short amphiphilic helices: a mutational analysis of the binding site of annexin II for p11. EMBO J. 9, 4207-4213 (Pubitemid 120025975)
    • (1990) EMBO Journal , vol.9 , Issue.13 , pp. 4207-4213
    • Becker, T.1    Weber, K.2    Johnsson, N.3
  • 51
    • 33645515011 scopus 로고    scopus 로고
    • Dimerization and ion binding properties of S100P protein
    • Tutar, Y. (2006) Dimerization and ion binding properties of S100P protein. Protein Pept. Lett. 13, 301-306
    • (2006) Protein Pept. Lett. , vol.13 , pp. 301-306
    • Tutar, Y.1
  • 52
    • 0031658212 scopus 로고    scopus 로고
    • Hydrophobic residues in the C-terminal region of S100A1 are essential for target protein binding but not for dimerization
    • Osterloh, D., Ivanenkov, V. V. and Gerke, V. (1998) Hydrophobic residues in the C-terminal region of S100A1 are essential for target protein binding but not for dimerization. Cell Calcium 24, 137-151
    • (1998) Cell Calcium , vol.24 , pp. 137-151
    • Osterloh, D.1    Ivanenkov, V.V.2    Gerke, V.3
  • 53
    • 0034622580 scopus 로고    scopus 로고
    • Identification of hydrophobic amino acid residues involved in the formation of S100P homodimers in vivo
    • Koltzscher, M. and Gerke, V. (2000) Identification of hydrophobic amino acid residues involved in the formation of S100P homodimers in vivo. Biochemistry 39, 9533-9539
    • (2000) Biochemistry , vol.39 , pp. 9533-9539
    • Koltzscher, M.1    Gerke, V.2
  • 54
    • 1642494623 scopus 로고    scopus 로고
    • 15N multiple-quantum relaxation using field-dependent measurements: Time scale and structural characterization of exchange in a calmodulin C-terminal domain mutant
    • 15N multiple-quantum relaxation using field-dependent measurements: time scale and structural characterization of exchange in a calmodulin C-terminal domain mutant. J. Am. Chem. Soc. 126, 928-935
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 928-935
    • Lundstrom, P.1    Akke, M.2
  • 57
    • 0035078116 scopus 로고    scopus 로고
    • Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant
    • Evenas, J., Malmendal, A. and Akke, M. (2001) Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant. Structure 9, 185-195
    • (2001) Structure , vol.9 , pp. 185-195
    • Evenas, J.1    Malmendal, A.2    Akke, M.3
  • 58
    • 0033546403 scopus 로고    scopus 로고
    • Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations
    • Evenas, J., Forsen, S., Malmendal, A. and Akke, M. (1999) Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations. J. Mol. Biol. 289, 603-617
    • (1999) J. Mol. Biol. , vol.289 , pp. 603-617
    • Evenas, J.1    Forsen, S.2    Malmendal, A.3    Akke, M.4
  • 59
    • 0035940513 scopus 로고    scopus 로고
    • Long-range effects on calcium binding and conformational change in the N-domain of calmodulin
    • Ababou, A., Shenvi, R. A. and Desjarlais, J. R. (2001) Long-range effects on calcium binding and conformational change in the N-domain of calmodulin. Biochemistry 40, 12719-12726
    • (2001) Biochemistry , vol.40 , pp. 12719-12726
    • Ababou, A.1    Shenvi, R.A.2    Desjarlais, J.R.3
  • 60
    • 0035107931 scopus 로고    scopus 로고
    • Solvation energetics and conformational change in EF-hand proteins
    • Ababou, A. and Desjarlais, J. R. (2001) Solvation energetics and conformational change in EF-hand proteins. Protein Sci. 10, 301-312
    • (2001) Protein Sci. , vol.10 , pp. 301-312
    • Ababou, A.1    Desjarlais, J.R.2
  • 61
    • 0034680341 scopus 로고    scopus 로고
    • 2+and troponin I peptide binding to the E41A mutant of the N-domain of skeletal troponin C
    • 2+ and troponin I peptide binding to the E41A mutant of the N-domain of skeletal troponin C. Biochemistry 39, 12731-12738
    • (2000) Biochemistry , vol.39 , pp. 12731-12738
    • McKay, R.T.1    Saltibus, L.F.2    Li, M.X.3    Sykes, B.D.4
  • 62
    • 0030936958 scopus 로고    scopus 로고
    • Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins
    • Gagne, S. M., Li, M. X. and Sykes, B. D. (1997) Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins. Biochemistry 36, 4386-4392
    • (1997) Biochemistry , vol.36 , pp. 4386-4392
    • Gagne, S.M.1    Li, M.X.2    Sykes, B.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.