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Volumn 408, Issue 1, 2011, Pages 135-146

Simultaneous Formation of Right- and Left-handed Anti-parallel Coiled-coil Interfaces by a Coil2 Fragment of Human Lamin A

Author keywords

filament assembly; intermediate filaments; left handed coiled coil; nuclear lamins; right handed coiled coil

Indexed keywords

COILED COIL 2 PROTEIN; INTERMEDIATE FILAMENT PROTEIN; LAMIN A; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 79953242916     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.02.037     Document Type: Article
Times cited : (24)

References (48)
  • 2
    • 75649111950 scopus 로고    scopus 로고
    • Induction of a massive endoplasmic reticulum and perinuclear space expansion by expression of lamin B receptor mutants and the related sterol reductases TM7SF2 and DHCR7
    • Zwerger M., Kolb T., Richter K., Karakesisoglou I., and Herrmann H. Induction of a massive endoplasmic reticulum and perinuclear space expansion by expression of lamin B receptor mutants and the related sterol reductases TM7SF2 and DHCR7 Mol. Biol. Cell 21 2010 354 368
    • (2010) Mol. Biol. Cell , vol.21 , pp. 354-368
    • Zwerger, M.1    Kolb, T.2    Richter, K.3    Karakesisoglou, I.4    Herrmann, H.5
  • 3
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate Filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • DOI 10.1146/annurev.biochem.73.011303.073823
    • Herrmann H., and Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds Annu. Rev. Biochem. 73 2004 749 789 (Pubitemid 39050385)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 4
    • 33845286555 scopus 로고    scopus 로고
    • Human laminopathies: Nuclei gone genetically awry
    • DOI 10.1038/nrg1906, PII NRG1906
    • Capell B.C., and Collins F.S. Human laminopathies: nuclei gone genetically awry Nat. Rev. Genet. 7 2006 940 952 (Pubitemid 44871397)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.12 , pp. 940-952
    • Capell, B.C.1    Collins, F.S.2
  • 5
    • 84878091268 scopus 로고    scopus 로고
    • Emery-Dreifuss muscular dystrophy
    • Bonne G., Leturcq F., and Ben Yaou R. Emery-Dreifuss muscular dystrophy R.A. Pagon, T.C. Bird, C.R. Dolan, K. Stephens, GeneReviews [Internet] 2010 University of Washington Seattle, WA NCBI bookshelf ID, NBK1436; PMID, 20301609
    • (2010) GeneReviews [Internet]
    • Bonne, G.1    Leturcq, F.2    Ben Yaou, R.3
  • 6
    • 68849119046 scopus 로고    scopus 로고
    • Laminopathies and the long strange trip from basic cell biology to therapy
    • Worman H.J., Fong L.G., Muchir A., and Young S.G. Laminopathies and the long strange trip from basic cell biology to therapy J. Clin. Invest. 119 2009 1825 1836
    • (2009) J. Clin. Invest. , vol.119 , pp. 1825-1836
    • Worman, H.J.1    Fong, L.G.2    Muchir, A.3    Young, S.G.4
  • 10
    • 68849112456 scopus 로고    scopus 로고
    • Intermediate filaments: Primary determinants of cell architecture and plasticity
    • Herrmann H., Strelkov S.V., Burkhard P., and Aebi U. Intermediate filaments: primary determinants of cell architecture and plasticity J. Clin. Invest. 119 2009 1172 1183
    • (2009) J. Clin. Invest. , vol.119 , pp. 1172-1183
    • Herrmann, H.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4
  • 11
    • 5144220584 scopus 로고    scopus 로고
    • Crystal structure of the human lamin a coil 2B dimer: Implications for the head-to-tail association of nuclear lamins
    • DOI 10.1016/j.jmb.2004.08.093, PII S0022283604011040
    • Strelkov S.V., Schumacher J., Burkhard P., Aebi U., and Herrmann H. Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins J. Mol. Biol. 343 2004 1067 1080 (Pubitemid 39345965)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.4 , pp. 1067-1080
    • Strelkov, S.V.1    Schumacher, J.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 15
    • 0020338526 scopus 로고
    • The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins
    • Geisler N., and Weber K. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins EMBO J. 1 1982 1649 1656
    • (1982) EMBO J. , vol.1 , pp. 1649-1656
    • Geisler, N.1    Weber, K.2
  • 16
    • 0034685607 scopus 로고    scopus 로고
    • The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly
    • Herrmann H., Strelkov S.V., Feja B., Rogers K.R., Brettel M., and Lustig A. The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly J. Mol. Biol. 19 2000 817 832
    • (2000) J. Mol. Biol. , vol.19 , pp. 817-832
    • Herrmann, H.1    Strelkov, S.V.2    Feja, B.3    Rogers, K.R.4    Brettel, M.5    Lustig, A.6
  • 17
    • 77949316044 scopus 로고    scopus 로고
    • Characterization of the head-to-tail overlap complexes formed by human lamin A, B1 and B2 "mini-lamin" dimers
    • Kapinos L.E., Schumacher J., Mücke N., Machaidze G., Burkhard P., and Aebi U. Characterization of the head-to-tail overlap complexes formed by human lamin A, B1 and B2 "mini-lamin" dimers J. Mol. Biol. 396 2010 719 731
    • (2010) J. Mol. Biol. , vol.396 , pp. 719-731
    • Kapinos, L.E.1    Schumacher, J.2    Mücke, N.3    MacHaidze, G.4    Burkhard, P.5    Aebi, U.6
  • 18
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi U., Cohn J., Buhle L., and Gerace L The nuclear lamina is a meshwork of intermediate-type filaments Nature 323 1986 560 564 (Pubitemid 16025383)
    • (1986) Nature , vol.323 , Issue.6088 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 19
    • 0025804024 scopus 로고
    • 2 in Escherichia coli: Characterization of its structure, assembly, and molecular interactions
    • Heitlinger E., Peter M., Häner M., Lustig A., Aebi U., and Nigg E. Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions J. Cell Biol. 113 1991 485 495 (Pubitemid 21926006)
    • (1991) Journal of Cell Biology , vol.113 , Issue.3 , pp. 485-495
    • Heitlinger, E.1    Peter, M.2    Haner, M.3    Lustig, A.4    Aebi, U.5    Nigg, E.A.6
  • 20
    • 0026568833 scopus 로고
    • The role of the head and tail domain in lamin structure and assembly: Analysis of bacterially expressed chicken lamin A and truncated B2 lamins
    • Heitlinger E., Peter M., Lustig A., Villiger W., Nigg E.A., and Aebi U. The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins J. Struct. Biol. 108 1992 74 89
    • (1992) J. Struct. Biol. , vol.108 , pp. 74-89
    • Heitlinger, E.1    Peter, M.2    Lustig, A.3    Villiger, W.4    Nigg, E.A.5    Aebi, U.6
  • 22
    • 73949136181 scopus 로고    scopus 로고
    • A progeria mutation reveals functions for lamin A in nuclear assembly, architecture, and chromosome organization
    • Taimen P., Pfleghaar K., Shimi T., Möller D., Ben-Harush K., and Erdos M.R. A progeria mutation reveals functions for lamin A in nuclear assembly, architecture, and chromosome organization Proc. Natl Acad. Sci. USA 106 2009 20788 20793
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 20788-20793
    • Taimen, P.1    Pfleghaar, K.2    Shimi, T.3    Möller, D.4    Ben-Harush, K.5    Erdos, M.R.6
  • 23
    • 17444414616 scopus 로고    scopus 로고
    • Microdissection of the sequence and structure of intermediate filament chains
    • DOI 10.1016/S0065-3233(05)70005-X, Fibrous Proteins Coiled-Coils, Collagen and Elastomers
    • Parry D.A. Microdissection of the sequence and structure of intermediate filament chains Adv. Protein Chem. 70 2005 113 142 (Pubitemid 40544782)
    • (2005) Advances in Protein Chemistry , vol.70 , pp. 113-142
    • Parry, D.A.D.1
  • 24
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel K., and Henrick K. Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 25
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • DOI 10.1006/jsbi.2002.4454
    • Strelkov S.V., and Burkhard P. Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation J. Struct. Biol. 137 2002 54 64 (Pubitemid 35430421)
    • (2002) Journal of Structural Biology , vol.137 , Issue.1-2 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 26
    • 0344628627 scopus 로고    scopus 로고
    • Historical review: Another 50th anniversary - New periodicities in coiled coils
    • DOI 10.1016/j.tibs.2003.10.008
    • Gruber M., and Lupas A.N. Historical review: another 50th anniversary - new periodicities in coiled coils Trends Biochem. Sci. 28 2003 679 685 (Pubitemid 37500903)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.12 , pp. 679-685
    • Gruber, M.1    Lupas, A.N.2
  • 28
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    • DOI 10.1016/S0969-2126(00)00100-3
    • Burkhard P., Kammerer R.A., Steinmetz M.O., Bourenkov G.P., and Aebi U. The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges Structure 8 2000 223 230 (Pubitemid 30148689)
    • (2000) Structure , vol.8 , Issue.3 , pp. 223-230
    • Burkhard, P.1    Kammerer, R.A.2    Steinmetz, M.O.3    Bourenkov, G.P.4    Aebi, U.5
  • 29
    • 0034492490 scopus 로고    scopus 로고
    • Design of a minimal protein oligomerization domain by a structural approach
    • Burkhard P., Meier M., and Lustig A. Design of a minimal protein oligomerization domain by a structural approach Protein Sci. 9 2000 2294 2301 (Pubitemid 32105711)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2294-2301
    • Burkhard, P.1    Meier, M.2    Lustig, A.3
  • 30
    • 67349199644 scopus 로고    scopus 로고
    • Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation
    • Meier M., Padilla G.P., Herrmann H., Wedig T., Hergt M., and Patel T.R. Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation J. Mol. Biol. 390 2009 245 261
    • (2009) J. Mol. Biol. , vol.390 , pp. 245-261
    • Meier, M.1    Padilla, G.P.2    Herrmann, H.3    Wedig, T.4    Hergt, M.5    Patel, T.R.6
  • 31
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly
    • DOI 10.1093/emboj/21.6.1255
    • Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U., and Burkhard P. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly EMBO J. 21 2002 1255 1266 (Pubitemid 34246505)
    • (2002) EMBO Journal , vol.21 , Issue.6 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5    Aebi, U.6    Burkhard, P.7
  • 32
    • 0034685607 scopus 로고    scopus 로고
    • The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly
    • Herrmann H., Strelkov S.V., Feja B., Rogers K.R., Brettel M., and Lustig A. The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly J. Mol. Biol. 298 2000 817 832
    • (2000) J. Mol. Biol. , vol.298 , pp. 817-832
    • Herrmann, H.1    Strelkov, S.V.2    Feja, B.3    Rogers, K.R.4    Brettel, M.5    Lustig, A.6
  • 33
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments
    • Steinert P.M., Marekov L.N., and Parry D.A. Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments J. Biol. Chem. 268 1993 24916 24925 (Pubitemid 23335510)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.33 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 34
    • 7244221578 scopus 로고    scopus 로고
    • Structural characterisation of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance
    • DOI 10.1074/jbc.M406257200
    • Hess J.F., Budamagunta M.S., Voss J.C., and FitzGerald P.G. Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance J. Biol. Chem. 279 2004 44841 44846 (Pubitemid 39430896)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44841-44846
    • Hess, J.F.1    Budamagunta, M.S.2    Voss, J.C.3    Fitzgerald, P.G.4
  • 35
    • 0033926099 scopus 로고    scopus 로고
    • Review: Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics
    • DOI 10.1006/jsbi.2000.4212
    • Dechat T., Vlcek S., and Foisner R. Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics J. Struct. Biol. 129 2000 335 345 (Pubitemid 30481375)
    • (2000) Journal of Structural Biology , vol.129 , Issue.2-3 , pp. 335-345
    • Dechat, T.1    Vlcek, S.2    Foisner, R.3
  • 36
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • DOI 10.1016/S0076-6879(97)76075-0
    • Doublié S. Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530 (Pubitemid 27085620)
    • (1997) Methods in Enzymology , vol.276 , pp. 523-530
    • Doublie, S.1
  • 37
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade M.A., Chacón P., Merelo J.J., and Morán F. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network Protein Eng. 6 1993 383 390 (Pubitemid 23197398)
    • (1993) Protein Engineering , vol.6 , Issue.4 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 38
    • 0035957225 scopus 로고    scopus 로고
    • Energetics of coiled coil folding: The nature of the transition states
    • DOI 10.1021/bi002161l
    • Bosshard H.R., Dürr E., Hitz T., and Jelesarov I. Energetics of coiled coil folding: the nature of the transition states Biochemistry 40 2001 3544 3552 (Pubitemid 32242811)
    • (2001) Biochemistry , vol.40 , Issue.12 , pp. 3544-3552
    • Bosshard, H.R.1    Durr, E.2    Hitz, T.3    Jelesarov, I.4
  • 39
    • 0036382925 scopus 로고    scopus 로고
    • Unfolding of a leucine zipper is not a simple two-state transition
    • Dragan A.I., and Privalov P.L. Unfolding of a leucine zipper is not a simple two-state transition J. Mol. Biol. 321 2002 891 908
    • (2002) J. Mol. Biol. , vol.321 , pp. 891-908
    • Dragan, A.I.1    Privalov, P.L.2
  • 40
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • DOI 10.1006/abio.2000.4480
    • Philo J.S. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions Anal. Biochem. 279 2000 151 163 (Pubitemid 30165003)
    • (2000) Analytical Biochemistry , vol.279 , Issue.2 , pp. 151-163
    • Philo, J.S.1
  • 42
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick G.M. A short history of SHELX Acta Crystallogr. A 64 2008 112 122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D 50 1994 760 763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 47
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate filaments
    • DOI 10.1002/bies.10246
    • Strelkov S.V, Herrmann H., and Aebi U. Molecular architecture of intermediate filaments BioEssays 25 2003 243 251 (Pubitemid 36314111)
    • (2003) BioEssays , vol.25 , Issue.3 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2    Aebi, U.3
  • 48
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., and Wang X. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids Nucleic Acids Res 35 2007 W375 W383 Web Server issue
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5    Wang, X.6


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