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Volumn 348, Issue 3, 2005, Pages 711-725

Solution structure of the ran-binding domain 2 of RanBP2 and its interaction with the C terminus of ran

Author keywords

NMR structure; Nucleocytoplasmic transport; Ran; Ran binding domain; RanBP2

Indexed keywords

PLECKSTRIN; RAN BINDING PROTEIN 2; RAN PROTEIN; UNCLASSIFIED DRUG;

EID: 17144377919     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.033     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • K. Weis Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle Cell 112 2003 441 451
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 2
    • 0038699131 scopus 로고    scopus 로고
    • The small GTPase Ran: Interpreting the signs
    • B.B. Quimby, and M. Dasso The small GTPase Ran: interpreting the signs Curr. Opin. Cell Biol. 15 2003 338 344
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 338-344
    • Quimby, B.B.1    Dasso, M.2
  • 3
    • 0142188569 scopus 로고    scopus 로고
    • Ran in the spindle checkpoint: A new function for a versatile GTPase
    • H.Y. Li, K. Cao, and Y. Zheng Ran in the spindle checkpoint: a new function for a versatile GTPase Trends Cell Biol. 13 2003 553 557
    • (2003) Trends Cell Biol. , vol.13 , pp. 553-557
    • Li, H.Y.1    Cao, K.2    Zheng, Y.3
  • 4
    • 0038701027 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Navigating the channel
    • J. Bednenko, G. Cingolani, and L. Gerace Nucleocytoplasmic transport: navigating the channel Traffic 4 2003 127 135
    • (2003) Traffic , vol.4 , pp. 127-135
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 5
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • H. Fried, and U. Kutay Nucleocytoplasmic transport: taking an inventory Cell Mol. Life Sci. 60 2003 1659 1688
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 7
    • 0036264236 scopus 로고    scopus 로고
    • Regulation of nuclear import and export by the GTPase Ran
    • S.M. Steggerda, and B.M. Paschal Regulation of nuclear import and export by the GTPase Ran Int. Rev. Cytol. 217 2002 41 91
    • (2002) Int. Rev. Cytol. , vol.217 , pp. 41-91
    • Steggerda, S.M.1    Paschal, B.M.2
  • 8
    • 0034760338 scopus 로고    scopus 로고
    • RanBP3 influences interactions between CRM1 and its nuclear protein export substrates
    • L. Englmeier, M. Fornerod, F.R. Bischoff, C. Petosa, I.W. Mattaj, and U. Kutay RanBP3 influences interactions between CRM1 and its nuclear protein export substrates EMBO Rep. 2 2001 926 932
    • (2001) EMBO Rep. , vol.2 , pp. 926-932
    • Englmeier, L.1    Fornerod, M.2    Bischoff, F.R.3    Petosa, C.4    Mattaj, I.W.5    Kutay, U.6
  • 9
    • 0035954439 scopus 로고    scopus 로고
    • Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
    • M.E. Lindsay, J.M. Holaska, K. Welch, B.M. Paschal, and I.G. Macara Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export J. Cell Biol. 153 2001 1391 1402
    • (2001) J. Cell Biol. , vol.153 , pp. 1391-1402
    • Lindsay, M.E.1    Holaska, J.M.2    Welch, K.3    Paschal, B.M.4    MacAra, I.G.5
  • 10
    • 0037047430 scopus 로고    scopus 로고
    • Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta- mediated nuclear protein import
    • M.E. Lindsay, K. Plafker, A.E. Smith, B.E. Clurman, and I.G. Macara Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import Cell 110 2002 349 360
    • (2002) Cell , vol.110 , pp. 349-360
    • Lindsay, M.E.1    Plafker, K.2    Smith, A.E.3    Clurman, B.E.4    MacAra, I.G.5
  • 11
    • 0029070074 scopus 로고
    • Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin a homologous domain, and a leucine-rich region
    • J. Wu, M.J. Matunis, D. Kraemer, G. Blobel, and E. Coutavas Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region J. Biol. Chem. 270 1995 14209 14213
    • (1995) J. Biol. Chem. , vol.270 , pp. 14209-14213
    • Wu, J.1    Matunis, M.J.2    Kraemer, D.3    Blobel, G.4    Coutavas, E.5
  • 13
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: Implications for nuclear transport
    • I.R. Vetter, C. Nowak, T. Nishimoto, J. Kuhlmann, and A. Wittinghofer Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport Nature 398 1999 39 46
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 14
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • R. Mahajan, C. Delphin, T. Guan, L. Gerace, and F. Melchior A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2 Cell 88 1997 97 107
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 15
    • 0037033983 scopus 로고    scopus 로고
    • RanGAP mediates GTP hydrolysis without an arginine finger
    • M.J. Seewald, C. Korner, A. Wittinghofer, and I.R. Vetter RanGAP mediates GTP hydrolysis without an arginine finger Nature 415 2002 662 666
    • (2002) Nature , vol.415 , pp. 662-666
    • Seewald, M.J.1    Korner, C.2    Wittinghofer, A.3    Vetter, I.R.4
  • 16
    • 0028929866 scopus 로고
    • Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form
    • K. Scheffzek, C. Klebe, K. Fritz-Wolf, W. Kabsch, and A. Wittinghofer Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form Nature 374 1995 378 381
    • (1995) Nature , vol.374 , pp. 378-381
    • Scheffzek, K.1    Klebe, C.2    Fritz-Wolf, K.3    Kabsch, W.4    Wittinghofer, A.5
  • 17
    • 0032545173 scopus 로고    scopus 로고
    • The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2)
    • M. Stewart, H.M. Kent, and A.J. McCoy The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2) J. Mol. Biol. 284 1998 1517 1527
    • (1998) J. Mol. Biol. , vol.284 , pp. 1517-1527
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 18
    • 0032478537 scopus 로고    scopus 로고
    • Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran
    • M. Stewart, H.M. Kent, and A.J. McCoy Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran J. Mol. Biol. 277 1998 635 646
    • (1998) J. Mol. Biol. , vol.277 , pp. 635-646
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 19
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp
    • Y.M. Chook, and G. Blobel Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp Nature 399 1999 230 237
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 20
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-Importin beta interaction at 2.3 Å resolution
    • I.R. Vetter, A. Arndt, U. Kutay, D. Gorlich, and A. Wittinghofer Structural view of the Ran-Importin beta interaction at 2.3 Å resolution Cell 97 1999 635 646
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 21
    • 0030870158 scopus 로고    scopus 로고
    • Dynamic and equilibrium studies on the interaction of Ran with its effector, RanBP1
    • J. Kuhlmann, I. Macara, and A. Wittinghofer Dynamic and equilibrium studies on the interaction of Ran with its effector, RanBP1 Biochemistry 36 1997 12027 12035
    • (1997) Biochemistry , vol.36 , pp. 12027-12035
    • Kuhlmann, J.1    MacAra, I.2    Wittinghofer, A.3
  • 22
    • 0036177354 scopus 로고    scopus 로고
    • Sequence-specific resonance assignment of the second Ran-binding domain of human RanBP2
    • R. Doker, X. Zhao, W. Kremer, B. Villa, J. Kuhlmann, and H.R. Kalbitzer Sequence-specific resonance assignment of the second Ran-binding domain of human RanBP2 J. Biomol. NMR 22 2002 185 186
    • (2002) J. Biomol. NMR , vol.22 , pp. 185-186
    • Doker, R.1    Zhao, X.2    Kremer, W.3    Villa, B.4    Kuhlmann, J.5    Kalbitzer, H.R.6
  • 23
    • 0034718525 scopus 로고    scopus 로고
    • Different structural and kinetic requirements for the interaction of Ran with the Ran-binding domains from RanBP2 and importin-beta
    • C.I. Villa Braslavsky, C. Nowak, D. Gorlich, A. Wittinghofer, and J. Kuhlmann Different structural and kinetic requirements for the interaction of Ran with the Ran-binding domains from RanBP2 and importin-beta Biochemistry 39 2000 11629 11639
    • (2000) Biochemistry , vol.39 , pp. 11629-11639
    • Villa Braslavsky, C.I.1    Nowak, C.2    Gorlich, D.3    Wittinghofer, A.4    Kuhlmann, J.5
  • 24
    • 0029026774 scopus 로고
    • The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1
    • S.A. Richards, K.M. Lounsbury, and I.G. Macara The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1 J. Biol. Chem. 270 1995 14405 14411
    • (1995) J. Biol. Chem. , vol.270 , pp. 14405-14411
    • Richards, S.A.1    Lounsbury, K.M.2    MacAra, I.G.3
  • 25
    • 0036308740 scopus 로고    scopus 로고
    • The C-terminal extension of the small GTPase Ran is essential for defining the GDP-bound form
    • J. Nilsson, K. Weis, and J. Kjems The C-terminal extension of the small GTPase Ran is essential for defining the GDP-bound form J. Mol. Biol. 318 2002 583 593
    • (2002) J. Mol. Biol. , vol.318 , pp. 583-593
    • Nilsson, J.1    Weis, K.2    Kjems, J.3
  • 27
    • 1842486886 scopus 로고    scopus 로고
    • Automated structure determination of proteins by NMR spectroscopy
    • W. Gronwald, and H.R. Kalbitzer Automated structure determination of proteins by NMR spectroscopy Prog. Nucl. Magn. Reson. Spectrosc. 44 2004 33 96
    • (2004) Prog. Nucl. Magn. Reson. Spectrosc. , vol.44 , pp. 33-96
    • Gronwald, W.1    Kalbitzer, H.R.2
  • 28
    • 0036700835 scopus 로고    scopus 로고
    • Automated assignment of NOESY NMR spectra using a knowledge based method (KNOWNOE)
    • W. Gronwald, S. Moussa, R. Elsner, A. Jung, B. Ganslmeier, and J. Trenner Automated assignment of NOESY NMR spectra using a knowledge based method (KNOWNOE) J. Biomol. NMR 23 2002 271 287
    • (2002) J. Biomol. NMR , vol.23 , pp. 271-287
    • Gronwald, W.1    Moussa, S.2    Elsner, R.3    Jung, A.4    Ganslmeier, B.5    Trenner, J.6
  • 32
    • 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. Rullmannn, 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    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 34
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations 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
  • 35
  • 36
    • 0037138381 scopus 로고    scopus 로고
    • PTB or not PTB - That is the question
    • K.S. Yan, M. Kuti, and M.M. Zhou PTB or not PTB - that is the question FEBS Letters 513 2002 67 70
    • (2002) FEBS Letters , vol.513 , pp. 67-70
    • Yan, K.S.1    Kuti, M.2    Zhou, M.M.3
  • 37
    • 1242263882 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates
    • D. Auguin, P. Barthe, M.T. Auge-Senegas, M.H. Stern, M. Noguchi, and C. Roumestand Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates J. Biomol. NMR 28 2004 137 155
    • (2004) J. Biomol. NMR , vol.28 , pp. 137-155
    • Auguin, D.1    Barthe, P.2    Auge-Senegas, M.T.3    Stern, M.H.4    Noguchi, M.5    Roumestand, C.6
  • 38
    • 0028836020 scopus 로고
    • Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy
    • D. Fushman, S. Cahill, M.A. Lemmon, J. Schlessinger, and D. Cowburn Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy Proc. Natl Acad. Sci. USA 92 1995 816 820
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 816-820
    • Fushman, D.1    Cahill, S.2    Lemmon, M.A.3    Schlessinger, J.4    Cowburn, D.5
  • 40
    • 0035847054 scopus 로고    scopus 로고
    • A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin beta, CRM1 and RanBP1
    • J. Nilsson, P. Askjaer, and J. Kjems A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin beta, CRM1 and RanBP1 J. Mol. Biol. 305 2001 231 243
    • (2001) J. Mol. Biol. , vol.305 , pp. 231-243
    • Nilsson, J.1    Askjaer, P.2    Kjems, J.3
  • 41
    • 0033593805 scopus 로고    scopus 로고
    • A monoclonal antibody to the COOH-terminal acidic portion of Ran inhibits both the recycling of Ran and nuclear protein import in living cells
    • M. Hieda, T. Tachibana, F. Yokoya, S. Kose, N. Imamoto, and Y. Yoneda A monoclonal antibody to the COOH-terminal acidic portion of Ran inhibits both the recycling of Ran and nuclear protein import in living cells J. Cell Biol. 144 1999 645 655
    • (1999) J. Cell Biol. , vol.144 , pp. 645-655
    • Hieda, M.1    Tachibana, T.2    Yokoya, F.3    Kose, S.4    Imamoto, N.5    Yoneda, Y.6
  • 42
    • 0037119367 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer biosensors that detect Ran conformational changes and a Ran x GDP-importin-beta -RanBP1 complex in vitro and in intact cells
    • K. Plafker, and I.G. Macara Fluorescence resonance energy transfer biosensors that detect Ran conformational changes and a Ran x GDP-importin-beta -RanBP1 complex in vitro and in intact cells J. Biol. Chem. 277 2002 30121 30127
    • (2002) J. Biol. Chem. , vol.277 , pp. 30121-30127
    • Plafker, K.1    MacAra, I.G.2
  • 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
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich 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


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