메뉴 건너뛰기




Volumn 21, Issue 8, 2013, Pages 1350-1360

Structural determinants and mechanism of mammalian CRM1 allostery

Author keywords

[No Author keywords available]

Indexed keywords

EXPORTIN 1;

EID: 84881477247     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.05.015     Document Type: Article
Times cited : (15)

References (44)
  • 4
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-βs: Recognition and inhibition
    • Y.M. Chook, and K.E. Süel Nuclear import by karyopherin-βs: recognition and inhibition Biochim. Biophys. Acta 1813 2011 1593 1606
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1593-1606
    • Chook, Y.M.1    Süel, K.E.2
  • 5
    • 77951299111 scopus 로고    scopus 로고
    • Nuclear export complexes in the frame
    • A.G. Cook, and E. Conti Nuclear export complexes in the frame Curr. Opin. Struct. Biol. 20 2010 247 252
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 247-252
    • Cook, A.G.1    Conti, E.2
  • 6
    • 20844458749 scopus 로고    scopus 로고
    • The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding
    • A. Cook, E. Fernandez, D. Lindner, J. Ebert, G. Schlenstedt, and E. Conti The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding Mol. Cell 18 2005 355 367
    • (2005) Mol. Cell , vol.18 , pp. 355-367
    • Cook, A.1    Fernandez, E.2    Lindner, D.3    Ebert, J.4    Schlenstedt, G.5    Conti, E.6
  • 7
    • 69949094998 scopus 로고    scopus 로고
    • Structures of the tRNA export factor in the nuclear and cytosolic states
    • A.G. Cook, N. Fukuhara, M. Jinek, and E. Conti Structures of the tRNA export factor in the nuclear and cytosolic states Nature 461 2009 60 65
    • (2009) Nature , vol.461 , pp. 60-65
    • Cook, A.G.1    Fukuhara, N.2    Jinek, M.3    Conti, E.4
  • 8
    • 66149092358 scopus 로고    scopus 로고
    • Structural basis for assembly and disassembly of the CRM1 nuclear export complex
    • X. Dong, A. Biswas, and Y.M. Chook Structural basis for assembly and disassembly of the CRM1 nuclear export complex Nat. Struct. Mol. Biol. 16 2009 558 560
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 558-560
    • Dong, X.1    Biswas, A.2    Chook, Y.M.3
  • 9
    • 67349140506 scopus 로고    scopus 로고
    • Structural basis for leucine-rich nuclear export signal recognition by CRM1
    • X. Dong, A. Biswas, K.E. Süel, L.K. Jackson, R. Martinez, H. Gu, and Y.M. Chook Structural basis for leucine-rich nuclear export signal recognition by CRM1 Nature 458 2009 1136 1141
    • (2009) Nature , vol.458 , pp. 1136-1141
    • Dong, X.1    Biswas, A.2    Süel, K.E.3    Jackson, L.K.4    Martinez, R.5    Gu, H.6    Chook, Y.M.7
  • 11
    • 0034646565 scopus 로고    scopus 로고
    • Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha
    • M.R. Fontes, T. Teh, and B. Kobe Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha J. Mol. Biol. 297 2000 1183 1194
    • (2000) J. Mol. Biol. , vol.297 , pp. 1183-1194
    • Fontes, M.R.1    Teh, T.2    Kobe, B.3
  • 12
    • 0031053791 scopus 로고    scopus 로고
    • The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88
    • M. Fornerod, J. van Deursen, S. van Baal, A. Reynolds, D. Davis, K.G. Murti, J. Fransen, and G. Grosveld The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88 EMBO J. 16 1997 807 816
    • (1997) EMBO J , vol.16 , pp. 807-816
    • Fornerod, M.1    Van Deursen, J.2    Van Baal, S.3    Reynolds, A.4    Davis, D.5    Murti, K.G.6    Fransen, J.7    Grosveld, G.8
  • 14
    • 80051674080 scopus 로고    scopus 로고
    • Electrostatic interactions involving the extreme C terminus of nuclear export factor CRM1 modulate its affinity for cargo
    • A.M. Fox, D. Ciziene, S.H. McLaughlin, and M. Stewart Electrostatic interactions involving the extreme C terminus of nuclear export factor CRM1 modulate its affinity for cargo J. Biol. Chem. 286 2011 29325 29335
    • (2011) J. Biol. Chem. , vol.286 , pp. 29325-29335
    • Fox, A.M.1    Ciziene, D.2    McLaughlin, S.H.3    Stewart, M.4
  • 15
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • D. Franke, and D.I. Svergun DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering J. Appl. Crystallogr. 42 2009 342 346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 16
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • R.A. Friesner, G.A. Kaminski, J. Tirado-Rives, and W.L. Jorgensen Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides J. Phys. Chem. B 105 2001 6474 6487
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Friesner, R.A.1    Kaminski, G.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 20
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 21
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • V. Hornak, R. Abel, A. Okur, B. Strockbine, A. Roitberg, and C. Simmerling Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65 2006 712 725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 22
    • 33947726050 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export: To the pore and beyond
    • S. Hutten, and R.H. Kehlenbach CRM1-mediated nuclear export: to the pore and beyond Trends Cell Biol. 17 2007 193 201
    • (2007) Trends Cell Biol. , vol.17 , pp. 193-201
    • Hutten, S.1    Kehlenbach, R.H.2
  • 24
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • W.L. Jorgensen, D.S. Maxwell, and J. TiradoRives Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids J. Am. Chem. Soc. 118 1996 11225 11236
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tiradorives, J.3
  • 25
    • 77956544822 scopus 로고    scopus 로고
    • An unusual hydrophobic core confers extreme flexibility to HEAT repeat proteins
    • C. Kappel, U. Zachariae, N. Dölker, and H. Grubmüller An unusual hydrophobic core confers extreme flexibility to HEAT repeat proteins Biophys. J. 99 2010 1596 1603
    • (2010) Biophys. J. , vol.99 , pp. 1596-1603
    • Kappel, C.1    Zachariae, U.2    Dölker, N.3    Grubmüller, H.4
  • 27
    • 77953617671 scopus 로고    scopus 로고
    • An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1
    • M. Koyama, and Y. Matsuura An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1 EMBO J. 29 2010 2002 2013
    • (2010) EMBO J , vol.29 , pp. 2002-2013
    • Koyama, M.1    Matsuura, Y.2
  • 29
    • 11144257756 scopus 로고    scopus 로고
    • Structural basis for the assembly of a nuclear export complex
    • Y. Matsuura, and M. Stewart Structural basis for the assembly of a nuclear export complex Nature 432 2004 872 877
    • (2004) Nature , vol.432 , pp. 872-877
    • Matsuura, Y.1    Stewart, M.2
  • 31
    • 66249108600 scopus 로고    scopus 로고
    • Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP
    • T. Monecke, T. Güttler, P. Neumann, A. Dickmanns, D. Görlich, and R. Ficner Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP Science 324 2009 1087 1091
    • (2009) Science , vol.324 , pp. 1087-1091
    • Monecke, T.1    Güttler, T.2    Neumann, P.3    Dickmanns, A.4    Görlich, D.5    Ficner, R.6
  • 36
    • 0028950991 scopus 로고
    • Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins
    • A. Radu, G. Blobel, and M.S. Moore Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins Proc. Natl. Acad. Sci. USA 92 1995 1769 1773
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1769-1773
    • Radu, A.1    Blobel, G.2    Moore, M.S.3
  • 37
    • 84872101305 scopus 로고    scopus 로고
    • A 2.1-Å-resolution crystal structure of unliganded CRM1 reveals the mechanism of autoinhibition
    • N. Saito, and Y. Matsuura A 2.1-Å-resolution crystal structure of unliganded CRM1 reveals the mechanism of autoinhibition J. Mol. Biol. 425 2013 350 364
    • (2013) J. Mol. Biol. , vol.425 , pp. 350-364
    • Saito, N.1    Matsuura, Y.2
  • 38
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 39
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • D.I. Svergun Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing Biophys. J. 76 1999 2879 2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 40
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • D.I. Svergun, and M.B. Kozin Automated matching of high- and low-resolution structural models J. Appl. Crystallogr. 34 2001 33 41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Svergun, D.I.1    Kozin, M.B.2
  • 41
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 42
    • 84858005605 scopus 로고    scopus 로고
    • Nuclear export of proteins and drug resistance in cancer
    • J.G. Turner, J. Dawson, and D.M. Sullivan Nuclear export of proteins and drug resistance in cancer Biochem. Pharmacol. 83 2012 1021 1032
    • (2012) Biochem. Pharmacol. , vol.83 , pp. 1021-1032
    • Turner, J.G.1    Dawson, J.2    Sullivan, D.M.3
  • 44
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 36 2003 860 864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.