메뉴 건너뛰기




Volumn 46, Issue 27, 2007, Pages 7980-7991

Conformational plasticity of the lipid transfer protein SCP2

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE HYDROGEN EXCHANGE; CONFORMATIONAL PLASTICITY; LIPID BINDING POCKET;

EID: 34447297842     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi6025616     Document Type: Article
Times cited : (20)

References (40)
  • 1
    • 0033118353 scopus 로고    scopus 로고
    • High-affinity binding of very-long-chain fatty acyl-CoA esters to the peroxisomal non-specific lipid-transfer protein (sterol carrier protein-2)
    • Dansen, T. B., Westerman, J., Wouters, F. S., Wanders, R. J., van Hoek, A., Gadella, T. W., Jr., and Wirtz, K. W. (1999) High-affinity binding of very-long-chain fatty acyl-CoA esters to the peroxisomal non-specific lipid-transfer protein (sterol carrier protein-2), Biochem. J. 339 (Part 1), 193-199.
    • (1999) Biochem. J , vol.339 , Issue.PART 1 , pp. 193-199
    • Dansen, T.B.1    Westerman, J.2    Wouters, F.S.3    Wanders, R.J.4    van Hoek, A.5    Gadella Jr., T.W.6    Wirtz, K.W.7
  • 2
    • 0029751076 scopus 로고    scopus 로고
    • Sterol carrier protein-2, a new fatty acyl coenzyme A-binding protein
    • Frolov, A., Cho, T. H., Billheimer, J. T., and Schroeder, F. (1996) Sterol carrier protein-2, a new fatty acyl coenzyme A-binding protein, J. Biol. Chem. 271, 31878-31884.
    • (1996) J. Biol. Chem , vol.271 , pp. 31878-31884
    • Frolov, A.1    Cho, T.H.2    Billheimer, J.T.3    Schroeder, F.4
  • 4
    • 0035930593 scopus 로고    scopus 로고
    • Disruption of the sterol carrier protein 2 gene in mice impairs biliary lipid and hepatic cholesterol metabolism
    • Fuchs, M., Hafer, A., Munch, C., Kannenberg, F., Teichmann, S., Scheibner, J., Stange, E. F., and Seedorf, U. (2001) Disruption of the sterol carrier protein 2 gene in mice impairs biliary lipid and hepatic cholesterol metabolism, J. Biol. Chem. 276, 48058-48065.
    • (2001) J. Biol. Chem , vol.276 , pp. 48058-48065
    • Fuchs, M.1    Hafer, A.2    Munch, C.3    Kannenberg, F.4    Teichmann, S.5    Scheibner, J.6    Stange, E.F.7    Seedorf, U.8
  • 5
    • 0019224561 scopus 로고
    • Purification and properties of sterol carrier protein2
    • Noland, B. J., Arebalo, R. E., Hansbury, E., and Scallen, T. J. (1980) Purification and properties of sterol carrier protein2, J. Biol. Chem. 255, 4282-4289.
    • (1980) J. Biol. Chem , vol.255 , pp. 4282-4289
    • Noland, B.J.1    Arebalo, R.E.2    Hansbury, E.3    Scallen, T.J.4
  • 7
    • 0037790917 scopus 로고    scopus 로고
    • The enzymes, regulation, and genetics of bile acid synthesis
    • Russell, D. W. (2003) The enzymes, regulation, and genetics of bile acid synthesis, Annu. Rev. Biochem. 72, 137-174.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 137-174
    • Russell, D.W.1
  • 11
    • 0141643114 scopus 로고    scopus 로고
    • The structural determination of an insect sterol carrier protein-2 with a ligand-bound C16 fatty acid at 1.35-Å resolution
    • Dyer, D. H., Lovell, S., Thoden, J. B., Holden, H. M., Rayment, I., and Lan, Q. (2003) The structural determination of an insect sterol carrier protein-2 with a ligand-bound C16 fatty acid at 1.35-Å resolution, J. Biol. Chem. 278, 39085-39091.
    • (2003) J. Biol. Chem , vol.278 , pp. 39085-39091
    • Dyer, D.H.1    Lovell, S.2    Thoden, J.B.3    Holden, H.M.4    Rayment, I.5    Lan, Q.6
  • 13
    • 0034728386 scopus 로고    scopus 로고
    • Structure of sterol carrier protein 2 at 1.8 Å resolution reveals a hydrophobic tunnel suitable for lipid binding
    • Choinowski, T., Hauser, H., and Piontek, K. (2000) Structure of sterol carrier protein 2 at 1.8 Å resolution reveals a hydrophobic tunnel suitable for lipid binding, Biochemistry 39, 1897-1902.
    • (2000) Biochemistry , vol.39 , pp. 1897-1902
    • Choinowski, T.1    Hauser, H.2    Piontek, K.3
  • 14
    • 0031872482 scopus 로고    scopus 로고
    • In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide is flexibly disordered, and residues 21-143 adopt the same globular fold as in mature SCP2)
    • Weber, F. E., Dyer, J. H., Garcia, F. L., Werder, M., Szyperski, T., and Wuthrich, K. (1998) In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide is flexibly disordered, and residues 21-143 adopt the same globular fold as in mature SCP2), Cell. Mol. Life Sci. 54, 751-759.
    • (1998) Cell. Mol. Life Sci , vol.54 , pp. 751-759
    • Weber, F.E.1    Dyer, J.H.2    Garcia, F.L.3    Werder, M.4    Szyperski, T.5    Wuthrich, K.6
  • 15
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto, G. J., Jr., Geisbrecht, B. V., Gould, S. J., and Berg, J. M. (2000) Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5, Nat. Struct. Biol. 7, 1091-1095.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1091-1095
    • Gatto Jr., G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 16
    • 18944372099 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes. Topogenesis of the peroxisomal membrane and matrix proteins
    • Heiland, I., and Erdmann, R. (2005) Biogenesis of peroxisomes. Topogenesis of the peroxisomal membrane and matrix proteins, FEBS J. 272, 2362-2372.
    • (2005) FEBS J , vol.272 , pp. 2362-2372
    • Heiland, I.1    Erdmann, R.2
  • 17
    • 0036394986 scopus 로고    scopus 로고
    • Response of SCP-2L domain of human MFE-2 to ligand removal: Binding site closure and burial of peroxisomal targeting signal
    • Lensink, M. F., Haapalainen, A. M., Hiltunen, J. K., Glumoff, T., and Juffer, A. H. (2002) Response of SCP-2L domain of human MFE-2 to ligand removal: binding site closure and burial of peroxisomal targeting signal, J. Mol. Biol. 323, 99-113.
    • (2002) J. Mol. Biol , vol.323 , pp. 99-113
    • Lensink, M.F.1    Haapalainen, A.M.2    Hiltunen, J.K.3    Glumoff, T.4    Juffer, A.H.5
  • 20
    • 11844253256 scopus 로고    scopus 로고
    • Synergistic use of synchrotron radiation techniques for biological samples in solution: A case study on protein-ligand recognition by the peroxisomal import receptor Pex5p
    • Stanley, W. A., Sokolova, A., Brown, A., Clarke, D. T., Wilmanns, M., and Svergun, D. I. (2004) Synergistic use of synchrotron radiation techniques for biological samples in solution: a case study on protein-ligand recognition by the peroxisomal import receptor Pex5p, J. Synchrotron Radiat. 11, 490-496.
    • (2004) J. Synchrotron Radiat , vol.11 , pp. 490-496
    • Stanley, W.A.1    Sokolova, A.2    Brown, A.3    Clarke, D.T.4    Wilmanns, M.5    Svergun, D.I.6
  • 21
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler, M., Schleucher, J. and Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients, Prog. NMR Spectrosc. 34, 93-158.
    • (1999) Prog. NMR Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 22
    • 4644246567 scopus 로고    scopus 로고
    • Noninvasive methods to determine the critical micelle concentration of some bile acid salts
    • Reis, S., Moutinho, C. G., Matos, C., de Castro, B., Gameiro, P., and Lima, J. L. (2004) Noninvasive methods to determine the critical micelle concentration of some bile acid salts, Anal. Biochem. 334, 117-126.
    • (2004) Anal. Biochem , vol.334 , pp. 117-126
    • Reis, S.1    Moutinho, C.G.2    Matos, C.3    de Castro, B.4    Gameiro, P.5    Lima, J.L.6
  • 25
    • 0000451529 scopus 로고    scopus 로고
    • Improved HSQC experiments for the observation of exchange broadened signals
    • Mulder, F. A., Spronk, C. A., Slijper, M., Kaptein, R., and Boelens, R. (1996) Improved HSQC experiments for the observation of exchange broadened signals, J. Biomol. NMR 8, 223-228.
    • (1996) J. Biomol. NMR , vol.8 , pp. 223-228
    • Mulder, F.A.1    Spronk, C.A.2    Slijper, M.3    Kaptein, R.4    Boelens, R.5
  • 26
  • 27
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • Battiste, J. L., and Wagner, G. (2000) Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data, Biochemistry 39, 5355-5365.
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 28
    • 0033544895 scopus 로고    scopus 로고
    • Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites
    • Stolowich, N., Frolov, A., Petrescu, A. D., Scott, A. I., Billheimer, J. T., and Schroeder, F. (1999) Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites, J. Biol. Chem. 274, 35425-35433.
    • (1999) J. Biol. Chem , vol.274 , pp. 35425-35433
    • Stolowich, N.1    Frolov, A.2    Petrescu, A.D.3    Scott, A.I.4    Billheimer, J.T.5    Schroeder, F.6
  • 30
    • 0032545169 scopus 로고    scopus 로고
    • Characterisation of low free-energy excited states of folded proteins
    • Baxter, N. J., Hosszu, L. L., Waltho, J. P., and Williamson, M. P. (1998) Characterisation of low free-energy excited states of folded proteins, J. Mol. Biol. 284, 1625-1639.
    • (1998) J. Mol. Biol , vol.284 , pp. 1625-1639
    • Baxter, N.J.1    Hosszu, L.L.2    Waltho, J.P.3    Williamson, M.P.4
  • 31
    • 0033003378 scopus 로고    scopus 로고
    • Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements
    • Mulder, F. A., van Tilborg, P. J., Kaptein, R., and Boelens, R. (1999) Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements, J. Biomol. NMR 13, 275-288.
    • (1999) J. Biomol. NMR , vol.13 , pp. 275-288
    • Mulder, F.A.1    van Tilborg, P.J.2    Kaptein, R.3    Boelens, R.4
  • 32
    • 16244365477 scopus 로고    scopus 로고
    • Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems
    • Palmer, A. G., III, Grey, M. J., and Wang, C. (2005) Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems, Methods Enzymol. 394, 430-465.
    • (2005) Methods Enzymol , vol.394 , pp. 430-465
    • Palmer III, A.G.1    Grey, M.J.2    Wang, C.3
  • 33
    • 0028860964 scopus 로고
    • Improved RNA structure determination by detection of NOE contacts to exchange-broadened amino protons
    • Mueller, L., Legault, P., and Pardi, A. (1995) Improved RNA structure determination by detection of NOE contacts to exchange-broadened amino protons, J. Am. Chem. Soc. 117, 11043-11048.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 11043-11048
    • Mueller, L.1    Legault, P.2    Pardi, A.3
  • 34
    • 85047669202 scopus 로고    scopus 로고
    • The targeting and assembly of peroxisomal proteins: Some old rules do not apply
    • McNew, J. A., and Goodman, J. M. (1996) The targeting and assembly of peroxisomal proteins: some old rules do not apply, Trends Biochem. Sci. 21, 54-58.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 54-58
    • McNew, J.A.1    Goodman, J.M.2
  • 35
    • 0029082055 scopus 로고
    • Probing the ligand binding sites of fatty acid and sterol carrier proteins: Effects of ethanol
    • Schroeder, F., Myers-Payne, S. C., Billheimer, J. T., and Wood, W. G. (1995) Probing the ligand binding sites of fatty acid and sterol carrier proteins: effects of ethanol, Biochemistry 34, 11919-11927.
    • (1995) Biochemistry , vol.34 , pp. 11919-11927
    • Schroeder, F.1    Myers-Payne, S.C.2    Billheimer, J.T.3    Wood, W.G.4
  • 36
    • 0035819455 scopus 로고    scopus 로고
    • Measurement of slow (μs-ras) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
    • Mulder, F. A., Skrynnikov, N. R., Hon, B., Dahlquist, F. W., and Kay, L. E. (2001) Measurement of slow (μs-ras) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme, J. Am. Chem. Soc. 123, 967-975.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 967-975
    • Mulder, F.A.1    Skrynnikov, N.R.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 37
    • 8444248261 scopus 로고    scopus 로고
    • Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid
    • Nichesola, D., Perduca, M., Capaldi, S., Carrizo, M. E., Righetti, P. G., and Monaco, H. L. (2004) Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid, Biochemistry 43, 14072-14079.
    • (2004) Biochemistry , vol.43 , pp. 14072-14079
    • Nichesola, D.1    Perduca, M.2    Capaldi, S.3    Carrizo, M.E.4    Righetti, P.G.5    Monaco, H.L.6
  • 39
    • 0033514406 scopus 로고    scopus 로고
    • Dynamics of palmitic acid complexed with rat intestinal fatty acid binding protein
    • Zhu, L., Kurian, E., Prendergast, F. G., and Kemple, M. D. (1999) Dynamics of palmitic acid complexed with rat intestinal fatty acid binding protein, Biochemistry 38, 1554-1561.
    • (1999) Biochemistry , vol.38 , pp. 1554-1561
    • Zhu, L.1    Kurian, E.2    Prendergast, F.G.3    Kemple, M.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.