메뉴 건너뛰기




Volumn 363, Issue 2, 2006, Pages 469-481

Engineering, Biophysical Characterisation and Binding Properties of a Soluble Mutant form of Annexin A2 Domain IV that Adopts a Partially Folded Conformation

Author keywords

Annexin A2; calcium; CD; domain IV; heparin

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; HEPARIN; LIPOCORTIN 2;

EID: 33748951928     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.042     Document Type: Article
Times cited : (15)

References (45)
  • 2
    • 0025038549 scopus 로고
    • The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity
    • Huber R., Schneider M., Mayr I., Römisch J., and Paques E.P. The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. FEBS Letters 275 (1990) 15-21
    • (1990) FEBS Letters , vol.275 , pp. 15-21
    • Huber, R.1    Schneider, M.2    Mayr, I.3    Römisch, J.4    Paques, E.P.5
  • 3
    • 0035936691 scopus 로고    scopus 로고
    • X-ray structure of full-length annexin 1 and implications for membrane aggregation
    • Rosengarth A., Gerke V., and Luecke H. X-ray structure of full-length annexin 1 and implications for membrane aggregation. J. Mol. Biol. 306 (2001) 489-498
    • (2001) J. Mol. Biol. , vol.306 , pp. 489-498
    • Rosengarth, A.1    Gerke, V.2    Luecke, H.3
  • 4
    • 0036794361 scopus 로고    scopus 로고
    • Cloning, purification and crystallization of full-length human annexin 2
    • Tran J.T., Rosengarth A., and Luecke H. Cloning, purification and crystallization of full-length human annexin 2. Acta Crystallog. sect. D 58 (2002) 1854-1857
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 1854-1857
    • Tran, J.T.1    Rosengarth, A.2    Luecke, H.3
  • 5
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V., and Moss S.E. Annexins: from structure to function. Physiol. Rev. 82 (2002) 331-371
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 6
    • 33748919166 scopus 로고    scopus 로고
    • 2. Does it induce membrane aggregation by a new multimeric state of the protein?
    • 2. Does it induce membrane aggregation by a new multimeric state of the protein?. Annexins 1 (2004) 129-136
    • (2004) Annexins , vol.1 , pp. 129-136
    • Rosengarth, A.1    Luecke, H.2
  • 8
    • 0030821003 scopus 로고    scopus 로고
    • Three-dimensional structure of annexins
    • Liemann S., and Huber R. Three-dimensional structure of annexins. Cell. Mol. Life Sci. 53 (1997) 516-521
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 516-521
    • Liemann, S.1    Huber, R.2
  • 11
    • 0022928659 scopus 로고
    • 2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core
    • 2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core. J. Biol. Chem. 261 (1986) 7247-7252
    • (1986) J. Biol. Chem. , vol.261 , pp. 7247-7252
    • Glenney, J.1
  • 14
    • 0032568860 scopus 로고    scopus 로고
    • Exploring the folding pathways of annexin I, a multidomain protein. I. Non-native structures stabilize the partially folded state of the isolated domain 2 of annexin I
    • Cordier-Ochsenbein F., Guerois R., Baleux F., Huynh-Dinh T., Lirsac P.N., Russo-Marie F., et al. Exploring the folding pathways of annexin I, a multidomain protein. I. Non-native structures stabilize the partially folded state of the isolated domain 2 of annexin I. J. Mol. Biol. 279 (1998) 1163-1175
    • (1998) J. Mol. Biol. , vol.279 , pp. 1163-1175
    • Cordier-Ochsenbein, F.1    Guerois, R.2    Baleux, F.3    Huynh-Dinh, T.4    Lirsac, P.N.5    Russo-Marie, F.6
  • 15
    • 0032569033 scopus 로고    scopus 로고
    • Exploring the folding pathways of annexin I, a multidomain protein. II. Hierarchy in domain folding propensities may govern the folding process
    • Cordier-Ochsenbein F., Guerois R., Russo-Marie F., Neumann J.M., and Sanson A. Exploring the folding pathways of annexin I, a multidomain protein. II. Hierarchy in domain folding propensities may govern the folding process. J. Mol. Biol. 279 (1998) 1177-1185
    • (1998) J. Mol. Biol. , vol.279 , pp. 1177-1185
    • Cordier-Ochsenbein, F.1    Guerois, R.2    Russo-Marie, F.3    Neumann, J.M.4    Sanson, A.5
  • 16
    • 0033433850 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the isolated domain 1 of annexin I
    • Huynh T., Musat G., Neumann J.M., Smith J.C., and Sanson A. Molecular dynamics simulations of the isolated domain 1 of annexin I. Theor. Chem. Acc. 101 (1999) 82-86
    • (1999) Theor. Chem. Acc. , vol.101 , pp. 82-86
    • Huynh, T.1    Musat, G.2    Neumann, J.M.3    Smith, J.C.4    Sanson, A.5
  • 17
    • 0033613858 scopus 로고    scopus 로고
    • NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit
    • Gao J., Li Y., and Yan H. NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit. J. Biol. Chem. 274 (1999) 2971-2977
    • (1999) J. Biol. Chem. , vol.274 , pp. 2971-2977
    • Gao, J.1    Li, Y.2    Yan, H.3
  • 19
    • 3242877433 scopus 로고    scopus 로고
    • Annexins-unique membrane binding proteins with diverse functions
    • Rescher U., and Gerke V. Annexins-unique membrane binding proteins with diverse functions. J. Cell Sci. 117 (2004) 2631-2639
    • (2004) J. Cell Sci. , vol.117 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 21
    • 0026623535 scopus 로고
    • A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling
    • Jones P.G., Moore G.J., and Waisman D.M. A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling. J. Biol. Chem. 267 (1992) 13993-13997
    • (1992) J. Biol. Chem. , vol.267 , pp. 13993-13997
    • Jones, P.G.1    Moore, G.J.2    Waisman, D.M.3
  • 22
    • 0035895949 scopus 로고    scopus 로고
    • The C terminus of annexin II mediates binding to F-actin
    • Filipenko N.R., and Waisman D.M. The C terminus of annexin II mediates binding to F-actin. J. Biol. Chem. 276 (2001) 5310-5315
    • (2001) J. Biol. Chem. , vol.276 , pp. 5310-5315
    • Filipenko, N.R.1    Waisman, D.M.2
  • 23
    • 0034659962 scopus 로고    scopus 로고
    • Annexin II is associated with mRNAs which may constitute a distinct subpopulation
    • Vedeler A., and Hollås H. Annexin II is associated with mRNAs which may constitute a distinct subpopulation. Biochem. J. 348 (2000) 565-572
    • (2000) Biochem. J. , vol.348 , pp. 565-572
    • Vedeler, A.1    Hollås, H.2
  • 26
    • 53149124391 scopus 로고    scopus 로고
    • Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein
    • Sachdev D., and Chirgwin J.M. Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein. J. Protein Chem. 18 (1999) 127-136
    • (1999) J. Protein Chem. , vol.18 , pp. 127-136
    • Sachdev, D.1    Chirgwin, J.M.2
  • 33
    • 0035148547 scopus 로고    scopus 로고
    • Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surfaces
    • Capila I., Hernaiz M.J., Mo Y.D., Mealy T.R., Campos B., Dedman J.R., et al. Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surfaces. Structure 9 (2001) 57-64
    • (2001) Structure , vol.9 , pp. 57-64
    • Capila, I.1    Hernaiz, M.J.2    Mo, Y.D.3    Mealy, T.R.4    Campos, B.5    Dedman, J.R.6
  • 34
    • 0022481031 scopus 로고
    • Primary structure of bovine calpactin I heavy chain (p36), a major cellular substrate for retroviral protein-tyrosine kinases: homology with the human phospholipase A2 inhibitor lipocortin
    • Kristensen T., Saris C.J., Hunter T., Hicks L.J., Noonan D.J., Glenney Jr. J.R., and Tack B.F. Primary structure of bovine calpactin I heavy chain (p36), a major cellular substrate for retroviral protein-tyrosine kinases: homology with the human phospholipase A2 inhibitor lipocortin. Biochemistry 25 (1986) 4497-4503
    • (1986) Biochemistry , vol.25 , pp. 4497-4503
    • Kristensen, T.1    Saris, C.J.2    Hunter, T.3    Hicks, L.J.4    Noonan, D.J.5    Glenney Jr., J.R.6    Tack, B.F.7
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0042386147 scopus 로고    scopus 로고
    • Combination of two matrices results in improved performance of MALDI MS for peptide mass mapping and protein analysis
    • Laugesen S., and Roepstorff P. Combination of two matrices results in improved performance of MALDI MS for peptide mass mapping and protein analysis. J. Am. Soc. Mass Spectrom. 14 (2003) 992-1002
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 992-1002
    • Laugesen, S.1    Roepstorff, P.2
  • 37
    • 0038024376 scopus 로고    scopus 로고
    • Screening methods to determine biophysical properties of proteins in structural genomics
    • Woestenenk E.A., Hammarström M., Härd T., and Berglund H. Screening methods to determine biophysical properties of proteins in structural genomics. Anal. Biochem. 318 (2003) 71-79
    • (2003) Anal. Biochem. , vol.318 , pp. 71-79
    • Woestenenk, E.A.1    Hammarström, M.2    Härd, T.3    Berglund, H.4
  • 38
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., and Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2 (1992) 661-665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 39
    • 2642628181 scopus 로고
    • A two-dimensional nuclear overhauser experiment with pure absorption phase in 4 quadrants
    • States D.J., Haberkorn R.A., and Ruben D.J. A two-dimensional nuclear overhauser experiment with pure absorption phase in 4 quadrants. J. Magn. Reson. 48 (1982) 286-292
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 41
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules
    • Bartels C., Xia T.H., Billeter M., Güntert P., and Wüthrich K. The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules. J. Biomol. NMR 6 (1995) 1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 42
    • 33748947734 scopus 로고    scopus 로고
    • NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides
    • Vanhaverbeke C., Simorre J.P., Sadir R., Gans P., and Lortat-Jacob H. NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides. FEBS Letters 446 (1999) 446327-446330
    • (1999) FEBS Letters , vol.446 , pp. 446327-446330
    • Vanhaverbeke, C.1    Simorre, J.P.2    Sadir, R.3    Gans, P.4    Lortat-Jacob, H.5
  • 43
    • 0021118508 scopus 로고
    • Principles that determine the structure of proteins
    • Chothia C. Principles that determine the structure of proteins. Annu. Rev. Biochem. 53 (1984) 537-572
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 537-572
    • Chothia, C.1
  • 44
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8 (1990) 52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 45
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.