메뉴 건너뛰기




Volumn 113, Issue 29, 2016, Pages 8212-8217

Structure of human Niemann-Pick C1 protein

Author keywords

Allostery; Cholesterol traffic; Crystal structure; Endosomal membrane; Sterol sensing domain

Indexed keywords

CELL MEMBRANE PROTEIN; CHOLESTEROL; NIEMANN PICK C1 PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; COMPLEMENTARY DNA; MEMBRANE PROTEIN; NPC1 PROTEIN, HUMAN;

EID: 84978909337     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1607795113     Document Type: Article
Times cited : (133)

References (50)
  • 1
    • 77955053533 scopus 로고    scopus 로고
    • Cholesterol, the central lipid of mammalian cells
    • Maxfield FR, van Meer G (2010) Cholesterol, the central lipid of mammalian cells. Curr Opin Cell Biol 22(4):422-429.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.4 , pp. 422-429
    • Maxfield, F.R.1    Van Meer, G.2
  • 2
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS, Goldstein JL (1986) A receptor-mediated pathway for cholesterol homeostasis. Science 232(4746):34-47.
    • (1986) Science , vol.232 , Issue.4746 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 3
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signaling proteins in animal development
    • Porter JA, Young KE, Beachy PA (1996) Cholesterol modification of hedgehog signaling proteins in animal development. Science 274(5285):255-259.
    • (1996) Science , vol.274 , Issue.5285 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 5
    • 84923196528 scopus 로고    scopus 로고
    • Structure of an integral membrane sterol reductase from Methylomicrobium alcaliphilum
    • Li X, Roberti R, Blobel G (2015) Structure of an integral membrane sterol reductase from Methylomicrobium alcaliphilum. Nature 517(7532):104-107.
    • (2015) Nature , vol.517 , Issue.7532 , pp. 104-107
    • Li, X.1    Roberti, R.2    Blobel, G.3
  • 6
    • 0030298339 scopus 로고    scopus 로고
    • Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein
    • Hua X, Nohturfft A, Goldstein JL, Brown MS (1996) Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell 87(3):415-426.
    • (1996) Cell , vol.87 , Issue.3 , pp. 415-426
    • Hua, X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 7
    • 0036534286 scopus 로고    scopus 로고
    • The sterol-sensing domain: Multiple families, a unique role?
    • Kuwabara PE, Labouesse M (2002) The sterol-sensing domain: Multiple families, a unique role? Trends Genet 18(4):193-201.
    • (2002) Trends Genet , vol.18 , Issue.4 , pp. 193-201
    • Kuwabara, P.E.1    Labouesse, M.2
  • 8
    • 30344473341 scopus 로고    scopus 로고
    • Protein sensors for membrane sterols
    • Goldstein JL, DeBose-Boyd RA, Brown MS (2006) Protein sensors for membrane sterols. Cell 124(1):35-46.
    • (2006) Cell , vol.124 , Issue.1 , pp. 35-46
    • Goldstein, J.L.1    DeBose-Boyd, R.A.2    Brown, M.S.3
  • 9
    • 0030863352 scopus 로고    scopus 로고
    • Niemann-Pick C1 disease gene: Homology to mediators of cholesterol homeostasis
    • Carstea ED, et al. (1997) Niemann-Pick C1 disease gene: Homology to mediators of cholesterol homeostasis. Science 277(5323):228-231.
    • (1997) Science , vol.277 , Issue.5323 , pp. 228-231
    • Carstea, E.D.1
  • 10
    • 33644847857 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis before fluorescent proteins
    • Roth MG (2006) Clathrin-mediated endocytosis before fluorescent proteins. Nat Rev Mol Cell Biol 7(1):63-68.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.1 , pp. 63-68
    • Roth, M.G.1
  • 11
    • 0016836751 scopus 로고
    • Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease
    • Goldstein JL, Dana SE, Faust JR, Beaudet AL, Brown MS (1975) Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease. J Biol Chem 250(21):8487-8495.
    • (1975) J Biol Chem , vol.250 , Issue.21 , pp. 8487-8495
    • Goldstein, J.L.1    Dana, S.E.2    Faust, J.R.3    Beaudet, A.L.4    Brown, M.S.5
  • 12
    • 5044222456 scopus 로고    scopus 로고
    • Lysosomal acid lipase and atherosclerosis
    • Du H, Grabowski GA (2004) Lysosomal acid lipase and atherosclerosis. Curr Opin Lipidol 15(5):539-544.
    • (2004) Curr Opin Lipidol , vol.15 , Issue.5 , pp. 539-544
    • Du, H.1    Grabowski, G.A.2
  • 13
    • 0034704245 scopus 로고    scopus 로고
    • Identification of HE1 as the second gene of Niemann-Pick C disease
    • Naureckiene S, et al. (2000) Identification of HE1 as the second gene of Niemann-Pick C disease. Science 290(5500):2298-2301.
    • (2000) Science , vol.290 , Issue.5500 , pp. 2298-2301
    • Naureckiene, S.1
  • 14
    • 34548192003 scopus 로고    scopus 로고
    • Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease
    • Xu S, Benoff B, Liou HL, Lobel P, Stock AM (2007) Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease. J Biol Chem 282(32):23525-23531.
    • (2007) J Biol Chem , vol.282 , Issue.32 , pp. 23525-23531
    • Xu, S.1    Benoff, B.2    Liou, H.L.3    Lobel, P.4    Stock, A.M.5
  • 15
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • Kwon HJ, et al. (2009) Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol. Cell 137(7):1213-1224.
    • (2009) Cell , vol.137 , Issue.7 , pp. 1213-1224
    • Kwon, H.J.1
  • 16
    • 38149069055 scopus 로고    scopus 로고
    • Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein
    • Infante RE, et al. (2008) Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein. J Biol Chem 283(2):1052-1063.
    • (2008) J Biol Chem , vol.283 , Issue.2 , pp. 1052-1063
    • Infante, R.E.1
  • 17
    • 38149068309 scopus 로고    scopus 로고
    • Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop
    • Infante RE, et al. (2008) Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop. J Biol Chem 283(2):1064-1075.
    • (2008) J Biol Chem , vol.283 , Issue.2 , pp. 1064-1075
    • Infante, R.E.1
  • 18
    • 4344637102 scopus 로고    scopus 로고
    • Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain
    • Ohgami N, et al. (2004) Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain. Proc Natl Acad Sci USA 101(34):12473-12478.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.34 , pp. 12473-12478
    • Ohgami, N.1
  • 19
    • 84955259695 scopus 로고    scopus 로고
    • Identification of NPC1 as the target of U18666A, an inhibitor of lysosomal cholesterol export and Ebola infection
    • Lu F, et al. (2015) Identification of NPC1 as the target of U18666A, an inhibitor of lysosomal cholesterol export and Ebola infection. eLife 4:4.
    • (2015) ELife , vol.4 , pp. 4
    • Lu, F.1
  • 20
    • 84875448226 scopus 로고    scopus 로고
    • Discovery of oxysterol-derived pharmacological chaperones for NPC1: Implication for the existence of second sterolbinding site
    • Ohgane K, Karaki F, Dodo K, Hashimoto Y (2013) Discovery of oxysterol-derived pharmacological chaperones for NPC1: Implication for the existence of second sterolbinding site. Chem Biol 20(3):391-402.
    • (2013) Chem Biol , vol.20 , Issue.3 , pp. 391-402
    • Ohgane, K.1    Karaki, F.2    Dodo, K.3    Hashimoto, Y.4
  • 21
    • 73949159934 scopus 로고    scopus 로고
    • Linear clinical progression, independent of age of onset, in Niemann-Pick disease, type C
    • Yanjanin NM, et al. (2010) Linear clinical progression, independent of age of onset, in Niemann-Pick disease, type C. Am J Med Genet B Neuropsychiatr Genet 153 B (1): 132-140.
    • (2010) Am J Med Genet B Neuropsychiatr Genet , vol.153 B , Issue.1 , pp. 132-140
    • Yanjanin, N.M.1
  • 22
    • 4944263713 scopus 로고    scopus 로고
    • Niemann-Pick C research from mouse to gene
    • Pentchev PG (2004) Niemann-Pick C research from mouse to gene. Biochim Biophys Acta 1685(1-3):3-7.
    • (2004) Biochim Biophys Acta , vol.1685 , Issue.1-3 , pp. 3-7
    • Pentchev, P.G.1
  • 23
    • 80052851832 scopus 로고    scopus 로고
    • Ebola virus entry requires the cholesterol transporter Niemann-Pick C1
    • Carette JE, et al. (2011) Ebola virus entry requires the cholesterol transporter Niemann-Pick C1. Nature 477(7364):340-343.
    • (2011) Nature , vol.477 , Issue.7364 , pp. 340-343
    • Carette, J.E.1
  • 24
    • 80052868218 scopus 로고    scopus 로고
    • Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection
    • Côté M, et al. (2011) Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature 477(7364):344-348.
    • (2011) Nature , vol.477 , Issue.7364 , pp. 344-348
    • Côté, M.1
  • 25
    • 84859907529 scopus 로고    scopus 로고
    • Ebola virus entry requires the host-programmed recognition of an intracellular receptor
    • Miller EH, et al. (2012) Ebola virus entry requires the host-programmed recognition of an intracellular receptor. EMBO J 31(8):1947-1960.
    • (2012) EMBO J , vol.31 , Issue.8 , pp. 1947-1960
    • Miller, E.H.1
  • 26
    • 84954245042 scopus 로고    scopus 로고
    • Ebola viral glycoprotein bound to its endosomal receptor Niemann-Pick C1
    • Wang H, et al. (2016) Ebola viral glycoprotein bound to its endosomal receptor Niemann-Pick C1. Cell 164(1-2):258-268.
    • (2016) Cell , vol.164 , Issue.1-2 , pp. 258-268
    • Wang, H.1
  • 27
    • 84975303912 scopus 로고    scopus 로고
    • Ebola virus entry into host cells: Identifying therapeutic strategies
    • Rhein BA, Maury WJ (2015) Ebola virus entry into host cells: Identifying therapeutic strategies. Curr Clin Microbiol Rep 2(3):115-124.
    • (2015) Curr Clin Microbiol Rep , vol.2 , Issue.3 , pp. 115-124
    • Rhein, B.A.1    Maury, W.J.2
  • 28
    • 84936947069 scopus 로고    scopus 로고
    • Niemann-pick C1 is essential for ebolavirus replication and pathogenesis in vivo
    • Herbert AS, et al. (2015) Niemann-pick C1 is essential for ebolavirus replication and pathogenesis in vivo. MBio 6(3):e00565-15.
    • (2015) MBio , vol.6 , Issue.3 , pp. e00565-e00615
    • Herbert, A.S.1
  • 29
    • 54049097435 scopus 로고    scopus 로고
    • BacMam system for high-level expression of recombinant soluble and membrane glycoproteins for structural studies
    • Dukkipati A, Park HH, Waghray D, Fischer S, Garcia KC (2008) BacMam system for high-level expression of recombinant soluble and membrane glycoproteins for structural studies. Protein Expr Purif 62(2):160-170.
    • (2008) Protein Expr Purif , vol.62 , Issue.2 , pp. 160-170
    • Dukkipati, A.1    Park, H.H.2    Waghray, D.3    Fischer, S.4    Garcia, K.C.5
  • 30
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris GM, et al. (2009) AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J Comput Chem 30(16):2785-2791.
    • (2009) J Comput Chem , vol.30 , Issue.16 , pp. 2785-2791
    • Morris, G.M.1
  • 31
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Web Server issue
    • Holm L, Rosenstrom P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-W549.
    • (2010) Nucleic Acids Res , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenstrom, P.2
  • 32
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S, Nakashima R, Yamashita E, Yamaguchi A (2002) Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419(6907):587-593.
    • (2002) Nature , vol.419 , Issue.6907 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 33
    • 84881474318 scopus 로고    scopus 로고
    • Structural basis for the inhibition of bacterial multidrug exporters
    • Nakashima R, et al. (2013) Structural basis for the inhibition of bacterial multidrug exporters. Nature 500(7460):102-106.
    • (2013) Nature , vol.500 , Issue.7460 , pp. 102-106
    • Nakashima, R.1
  • 34
    • 77957141422 scopus 로고    scopus 로고
    • Crystal structures of the CusA efflux pump suggest methioninemediated metal transport
    • Long F, et al. (2010) Crystal structures of the CusA efflux pump suggest methioninemediated metal transport. Nature 467(7314):484-488.
    • (2010) Nature , vol.467 , Issue.7314 , pp. 484-488
    • Long, F.1
  • 35
    • 79958281760 scopus 로고    scopus 로고
    • Structure and function of a membrane component SecDF that enhances protein export
    • Tsukazaki T, et al. (2011) Structure and function of a membrane component SecDF that enhances protein export. Nature 474(7350):235-238.
    • (2011) Nature , vol.474 , Issue.7350 , pp. 235-238
    • Tsukazaki, T.1
  • 36
    • 0033170990 scopus 로고    scopus 로고
    • The RND permease superfamily: An ancient, ubiquitous and diverse family that includes human disease and development proteins
    • Tseng TT, et al. (1999) The RND permease superfamily: An ancient, ubiquitous and diverse family that includes human disease and development proteins. J Mol Microbiol Biotechnol 1(1):107-125.
    • (1999) J Mol Microbiol Biotechnol , vol.1 , Issue.1 , pp. 107-125
    • Tseng, T.T.1
  • 37
    • 0034704244 scopus 로고    scopus 로고
    • Transmembrane molecular pump activity of Niemann-Pick C1 protein
    • Davies JP, Chen FW, Ioannou YA (2000) Transmembrane molecular pump activity of Niemann-Pick C1 protein. Science 290(5500):2295-2298.
    • (2000) Science , vol.290 , Issue.5500 , pp. 2295-2298
    • Davies, J.P.1    Chen, F.W.2    Ioannou, Y.A.3
  • 38
    • 10644239801 scopus 로고    scopus 로고
    • Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs
    • Adams CM, et al. (2004) Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs. J Biol Chem 279(50):52772-52780.
    • (2004) J Biol Chem , vol.279 , Issue.50 , pp. 52772-52780
    • Adams, C.M.1
  • 39
    • 0037245750 scopus 로고    scopus 로고
    • Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain
    • Sever N, Yang T, Brown MS, Goldstein JL, DeBose-Boyd RA (2003) Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain. Mol Cell 11(1):25-33.
    • (2003) Mol Cell , vol.11 , Issue.1 , pp. 25-33
    • Sever, N.1    Yang, T.2    Brown, M.S.3    Goldstein, J.L.4    DeBose-Boyd, R.A.5
  • 40
    • 82755197370 scopus 로고    scopus 로고
    • Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding
    • Deffieu MS, Pfeffer SR (2011) Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding. Proc Natl Acad Sci USA 108(47):18932-18936.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.47 , pp. 18932-18936
    • Deffieu, M.S.1    Pfeffer, S.R.2
  • 41
    • 84948702864 scopus 로고    scopus 로고
    • Glycosylation inhibition reduces cholesterol accumulation in NPC1 protein-deficient cells
    • Li J, Deffieu MS, Lee PL, Saha P, Pfeffer SR (2015) Glycosylation inhibition reduces cholesterol accumulation in NPC1 protein-deficient cells. Proc Natl Acad Sci USA 112(48):14876-14881.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.48 , pp. 14876-14881
    • Li, J.1    Deffieu, M.S.2    Lee, P.L.3    Saha, P.4    Pfeffer, S.R.5
  • 42
    • 0037591389 scopus 로고    scopus 로고
    • StAR-related lipid transfer (START) proteins: Mediators of intracellular lipid metabolism
    • Soccio RE, Breslow JL (2003) StAR-related lipid transfer (START) proteins: Mediators of intracellular lipid metabolism. J Biol Chem 278(25):22183-22186.
    • (2003) J Biol Chem , vol.278 , Issue.25 , pp. 22183-22186
    • Soccio, R.E.1    Breslow, J.L.2
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski ZMW (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.M.W.1
  • 46
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 47
    • 0002583957 scopus 로고
    • 'dm': An automated procedure for phase improvement by density modification
    • Cowtan K (1994) 'dm': An automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newslett J Prot Crystallogr 31:34-38.
    • (1994) Joint CCP4 ESF-EACBM Newslett J Prot Crystallogr , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 48
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 49
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 50
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.