메뉴 건너뛰기




Volumn 346, Issue 5, 2005, Pages 1381-1392

Solution structure of human saposin C in a detergent environment

Author keywords

Detergent micelles; Membrane interactions; Nuclear magnetic resonance; Protein structure; Saposin C

Indexed keywords

DETERGENT; DODECYL SULFATE SODIUM; MONOMER; PROTEIN; SAPOSIN B; SAPOSIN C; SPHINGOLIPID ACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 13844299352     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.045     Document Type: Article
Times cited : (59)

References (47)
  • 1
    • 0032744716 scopus 로고    scopus 로고
    • Sphingolipid hydrolases and activator proteins
    • U. Bierfreund, T. Kolter, and K. Sandhoff Sphingolipid hydrolases and activator proteins Methods Enzymol. 311 2000 255 276
    • (2000) Methods Enzymol. , vol.311 , pp. 255-276
    • Bierfreund, U.1    Kolter, T.2    Sandhoff, K.3
  • 2
    • 1142263116 scopus 로고    scopus 로고
    • Saposins facilitate CD1d-restricted presentation of exogenous lipid antigen to T cells
    • S.-J. Kang, and P. Cresswell Saposins facilitate CD1d-restricted presentation of exogenous lipid antigen to T cells Nature Immunol. 5 2004 175 181
    • (2004) Nature Immunol. , vol.5 , pp. 175-181
    • Kang, S.-J.1    Cresswell, P.2
  • 3
    • 9144256638 scopus 로고    scopus 로고
    • Editing of CD1d-bound lipid antigens by endosomal lipid transfer proteins
    • D. Zhou, C. Cantu, Y. Sagiv, N. Schrantz, A.B. Kulkarni, and Y. Qi Editing of CD1d-bound lipid antigens by endosomal lipid transfer proteins Science 303 2004 523 527
    • (2004) Science , vol.303 , pp. 523-527
    • Zhou, D.1    Cantu, C.2    Sagiv, Y.3    Schrantz, N.4    Kulkarni, A.B.5    Qi, Y.6
  • 4
    • 0027181185 scopus 로고
    • Binding of cerebrosides and sulfatides to saposin A-D
    • S. Soeda, M. Hiraiwa, J.S. O'Brien, and Y. Kishimoto Binding of cerebrosides and sulfatides to saposin A-D J. Biol. Chem. 268 1993 18519 18523
    • (1993) J. Biol. Chem. , vol.268 , pp. 18519-18523
    • Soeda, S.1    Hiraiwa, M.2    O'Brien, J.S.3    Kishimoto, Y.4
  • 5
    • 0027327260 scopus 로고
    • Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient
    • K. Ito, N. Takahashi, A. Takahashi, I. Shimada, Y. Arata, J.S. O'Brien, and Y. Kishimoto Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient Eur. J. Biochem. 215 1993 171 179
    • (1993) Eur. J. Biochem. , vol.215 , pp. 171-179
    • Ito, K.1    Takahashi, N.2    Takahashi, A.3    Shimada, I.4    Arata, Y.5    O'Brien, J.S.6    Kishimoto, Y.7
  • 7
    • 0029730641 scopus 로고    scopus 로고
    • Biosynthesis, processing, and targeting of sphingolipid activator protein (SAP) precursor in cultured human fibroblasts
    • G. Vielhaber, R. Hurwitz, and K. Sandhoff Biosynthesis, processing, and targeting of sphingolipid activator protein (SAP) precursor in cultured human fibroblasts J. Biol. Chem. 271 1996 32438 32446
    • (1996) J. Biol. Chem. , vol.271 , pp. 32438-32446
    • Vielhaber, G.1    Hurwitz, R.2    Sandhoff, K.3
  • 9
    • 0025897376 scopus 로고
    • Saposin proteins: Structure, function, and role in human lysosomal storage disorders
    • J.S. O'Brien, and Y. Kishimoto Saposin proteins: structure, function, and role in human lysosomal storage disorders FASEB J. 5 1991 301 308
    • (1991) FASEB J. , vol.5 , pp. 301-308
    • O'Brien, J.S.1    Kishimoto, Y.2
  • 10
    • 0028054985 scopus 로고
    • Mutations causing Gaucher disease
    • M. Horowitz, and A. Zimran Mutations causing Gaucher disease Hum. Mutat. 3 1994 1 11
    • (1994) Hum. Mutat. , vol.3 , pp. 1-11
    • Horowitz, M.1    Zimran, A.2
  • 11
    • 0029417339 scopus 로고
    • PH-dependent conformational properties of saposins and their interactions with phospholipid membranes
    • A.M. Vaccaro, F. Ciaffoni, M. Tatti, R. Salvioli, A. Barca, D. Tognozzi, and C. Scerch pH-dependent conformational properties of saposins and their interactions with phospholipid membranes J. Biol. Chem. 270 1995 30576 30580
    • (1995) J. Biol. Chem. , vol.270 , pp. 30576-30580
    • Vaccaro, A.M.1    Ciaffoni, F.2    Tatti, M.3    Salvioli, R.4    Barca, A.5    Tognozzi, D.6    Scerch, C.7
  • 13
    • 0027494660 scopus 로고
    • Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes
    • A.M. Vaccaro, M. Tatti, F. Ciaffoni, R. Salvioli, B. Maras, and A. Barca Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes FEBS Letters 336 1993 159 162
    • (1993) FEBS Letters , vol.336 , pp. 159-162
    • Vaccaro, A.M.1    Tatti, M.2    Ciaffoni, F.3    Salvioli, R.4    Maras, B.5    Barca, A.6
  • 15
    • 0034697239 scopus 로고    scopus 로고
    • Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids
    • R. Salvioli, M. Tatti, F. Ciaffoni, and A.M. Vaccaro Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids FEBS Letters 472 2000 17 21
    • (2000) FEBS Letters , vol.472 , pp. 17-21
    • Salvioli, R.1    Tatti, M.2    Ciaffoni, F.3    Vaccaro, A.M.4
  • 16
    • 0028023035 scopus 로고
    • Saposin C induces pH-dependent destabilization and fusion of phosphatidylserine-containing vesicles
    • A.M. Vaccaro, M. Tatti, F. Ciaffoni, R. Salvioli, A. Serafino, and A. Barca Saposin C induces pH-dependent destabilization and fusion of phosphatidylserine-containing vesicles FEBS Letters 349 1994 181 186
    • (1994) FEBS Letters , vol.349 , pp. 181-186
    • Vaccaro, A.M.1    Tatti, M.2    Ciaffoni, F.3    Salvioli, R.4    Serafino, A.5    Barca, A.6
  • 17
    • 0025321793 scopus 로고
    • Characterization of a mutation in a family with saposin B deficiency: A glycosylation site defect
    • K.A. Kretz, G.S. Carson, Y. Kishimoto, A.L. Fluharty, and J.S. O'Brien Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect Proc. Natl Acad. Sci. USA 87 1990 2541 2544
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2541-2544
    • Kretz, K.A.1    Carson, G.S.2    Kishimoto, Y.3    Fluharty, A.L.4    O'Brien, J.S.5
  • 18
    • 0347625853 scopus 로고    scopus 로고
    • Solution structure of human saposin C: PH-dependent interaction with phospholipid vesicles
    • E. de Alba, S. Weiler, and N. Tjandra Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles Biochemistry 42 2003 14729 14740
    • (2003) Biochemistry , vol.42 , pp. 14729-14740
    • De Alba, E.1    Weiler, S.2    Tjandra, N.3
  • 20
    • 43949165935 scopus 로고
    • Effect of detergent concentration on multidimensional solution NMR spectra of membrane proteins in micelles
    • P.A. McDonnell, and S.J. Opella Effect of detergent concentration on multidimensional solution NMR spectra of membrane proteins in micelles J. Magn. Reson. 102 1993 120 125
    • (1993) J. Magn. Reson. , vol.102 , pp. 120-125
    • McDonnell, P.A.1    Opella, S.J.2
  • 21
    • 0028672795 scopus 로고
    • Methods to study membrane protein structure in solution
    • G.D. Henry, and B.D. Sykes Methods to study membrane protein structure in solution Methods Enzymol. 239 1994 515 535
    • (1994) Methods Enzymol. , vol.239 , pp. 515-535
    • Henry, G.D.1    Sykes, B.D.2
  • 22
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigation of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigation of nearest-neighbor effects J. Biomol. NMR 5 1995 67 81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 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
    • G.M. Clore, M.R. Starich, and A.M. Gronenborn 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 1998 10571 10572
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10571-10572
    • Clore, G.M.1    Starich, M.R.2    Gronenborn, A.M.3
  • 24
    • 0034066681 scopus 로고    scopus 로고
    • Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings
    • L.G. Barrientos, C. Dolan, and A.M. Gronenborn Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings J. Biomol. NMR 16 2000 329 337
    • (2000) J. Biomol. NMR , vol.16 , pp. 329-337
    • Barrientos, L.G.1    Dolan, C.2    Gronenborn, A.M.3
  • 25
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angle in biomolecules by NMR in a dilute liquid crystalline medium
    • N. Tjandra, and A. Bax Direct measurement of distances and angle in biomolecules by NMR in a dilute liquid crystalline medium Science 278 1997 1111 1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 26
    • 0034738066 scopus 로고    scopus 로고
    • Cellulose crystallites: A new and robust liquid crystalline medium for the measurement of residual dipolar couplings
    • K. Fleming, D. Gray, S. Prasannan, and S. Matthews Cellulose crystallites: a new and robust liquid crystalline medium for the measurement of residual dipolar couplings J. Am. Chem. Soc. 122 2000 5224 5225
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5224-5225
    • Fleming, K.1    Gray, D.2    Prasannan, S.3    Matthews, S.4
  • 27
    • 0035692486 scopus 로고    scopus 로고
    • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles
    • J.J. Chou, S. Gaemers, B. Howder, J.M. Louis, and A. Bax A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles J. Biomol. NMR 21 2001 377 382
    • (2001) J. Biomol. NMR , vol.21 , pp. 377-382
    • Chou, J.J.1    Gaemers, S.2    Howder, B.3    Louis, J.M.4    Bax, A.5
  • 28
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • G. Lipari, and A. Szabo Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity J. Am. Chem. Soc. 104 1982 4546 4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 29
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • G. Lipari, and A. Szabo Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results J. Am. Chem. Soc. 104 1982 4559 4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 33
    • 0028022578 scopus 로고
    • 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes
    • 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes FEBS Letters 350 1994 87 90
    • (1994) FEBS Letters , vol.350 , pp. 87-90
    • Lee, W.1    Revington, M.J.2    Arrowsmith, C.3    Kay, L.E.4
  • 34
    • 0035920203 scopus 로고    scopus 로고
    • Differential membrane interactions of saposins a and C
    • X. Qi, and G.A. Grabowski Differential membrane interactions of saposins A and C J. Biol. Chem. 276 2001 27010 27017
    • (2001) J. Biol. Chem. , vol.276 , pp. 27010-27017
    • Qi, X.1    Grabowski, G.A.2
  • 35
    • 0242488921 scopus 로고    scopus 로고
    • NMR solution structure determination of membrane proteins reconstituted in detergent micelles
    • C. Fernandez, and K. Wüthrich NMR solution structure determination of membrane proteins reconstituted in detergent micelles FEBS Letters 555 2003 144 150
    • (2003) FEBS Letters , vol.555 , pp. 144-150
    • Fernandez, C.1    Wüthrich, K.2
  • 36
    • 1642504446 scopus 로고    scopus 로고
    • Fusogenic domain and lysines in saposin C
    • X. Qi, and Z. Chu Fusogenic domain and lysines in saposin C Arch. Biochem. Biophys. 424 2004 210 218
    • (2004) Arch. Biochem. Biophys. , vol.424 , pp. 210-218
    • Qi, X.1    Chu, Z.2
  • 37
    • 2542620694 scopus 로고    scopus 로고
    • Characterization of a recombinant molecule covalently indistinguishable from human cerebroside-sulfate activator protein (CSAct or saposin B)
    • J.P. Whitelegge, V. Ahn, A.J. Norris, H. Sung, A. Waring, and R.L. Stevens Characterization of a recombinant molecule covalently indistinguishable from human cerebroside-sulfate activator protein (CSAct or saposin B) Cell. Mol. Biol. 49 2003 799 807
    • (2003) Cell. Mol. Biol. , vol.49 , pp. 799-807
    • Whitelegge, J.P.1    Ahn, V.2    Norris, A.J.3    Sung, H.4    Waring, A.5    Stevens, R.L.6
  • 38
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • E. Folta-Stogniew, and K.R. Williams Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory J. Biomol. Tech. 10 1999 51 63
    • (1999) J. Biomol. Tech. , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.R.2
  • 39
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • A. Bax, and S. Grzesiek Methodological advances in protein NMR Accts Chem. Res. 26 1993 131 138
    • (1993) Accts Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 40
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy
    • G. Barbato, M. Ikura, l.E. Kay, R.W. Pastor, and A. Bax Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy Biochemistry 31 1992 5269 5278
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 41
    • 0027787894 scopus 로고
    • The importance of not saturating water in protein NMR. Applications to sensitivity enhancement and NOE measurements
    • S. Grzesiek, and A. Bax The importance of not saturating water in protein NMR. Applications to sensitivity enhancement and NOE measurements J. Am. Chem. Soc. 115 1993 12593 12594
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 43
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams
    • D.S. Garrett, R. Powers, A.M. Gronenborn, and G.M. Clore A common sense approach to peak picking in two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams J. Magn. Reson. 95 1991 214 220
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 45
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 46
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A.C. Rullman, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullman, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wüthrich 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    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.