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Volumn 58, Issue 2, 2014, Pages 141-147

Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein

Author keywords

BLM; NMR structure; RecQ C terminal (RQC) domain; RecQ helicase

Indexed keywords

BLOOM SYNDROME HELICASE; DOUBLE STRANDED DNA; RECQ C TERMINAL; RECQ HELICASE; UNCLASSIFIED DRUG; WERNER SYNDROME PROTEIN;

EID: 84896735653     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-014-9812-8     Document Type: Article
Times cited : (7)

References (20)
  • 1
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E.coli RecQ helicase catalytic core
    • DOI 10.1093/emboj/cdg500
    • Bernstein DA, Zittel MC, Keck JL (2003) High-resolution structure of the E. coli RecQ helicase catalytic core. EMBO J 22(19):4910-4921. doi:10.1093/emboj/cdg500 (Pubitemid 37222013)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 4910-4921
    • Bernstein, D.A.1    Zittel, M.C.2    Keck, J.L.3
  • 2
    • 56449090762 scopus 로고    scopus 로고
    • Rising from the RecQ-age: The role of human RecQ helicases in genome maintenance
    • doi:10.1016/j.tibs.2008.09.003
    • Bohr VA (2008) Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance. Trends Biochem Sci 33(12): 609-620. doi:10.1016/j.tibs. 2008.09.003
    • (2008) Trends Biochem Sci , vol.33 , Issue.12 , pp. 609-620
    • Bohr, V.A.1
  • 3
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • doi:10.1038/nprot.2007.406
    • Brunger AT (2007) Version 1.2 of the crystallography and NMR system. Nat Protoc 2(11):2728-2733. doi:10.1038/nprot.2007.406
    • (2007) Nat Protoc , vol.2 , Issue.11 , pp. 2728-2733
    • Brunger, A.T.1
  • 5
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • doi:10.1385/1-59259-809-9:353
    • Guntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278:353-378. doi:10.1385/1-59259-809-9:353
    • (2004) Methods Mol Biol , vol.278 , pp. 353-378
    • Guntert, P.1
  • 6
    • 84879424236 scopus 로고    scopus 로고
    • From keys to bulldozers: Expanding roles for winged helix domains in nucleic-acid-binding proteins
    • doi:10.1016/j.tibs.2013.04.006
    • Harami GM, Gyimesi M, Kovacs M (2013) From keys to bulldozers: expanding roles for winged helix domains in nucleic-acid-binding proteins. Trends Biochem Sci 38(7):364-371. doi:10.1016/j.tibs.2013.04.006
    • (2013) Trends Biochem Sci , vol.38 , Issue.7 , pp. 364-371
    • Harami, G.M.1    Gyimesi, M.2    Kovacs, M.3
  • 8
    • 33646100776 scopus 로고    scopus 로고
    • A conserved G4 DNA binding domain in RecQ family helicases
    • doi:10.1016/j.jmb.2006.01.077
    • Huber MD, Duquette ML, Shiels JC, Maizels N (2006) A conserved G4 DNA binding domain in RecQ family helicases. J Mol Biol 358(4):1071-1080. doi:10.1016/j.jmb.2006.01.077
    • (2006) J Mol Biol , vol.358 , Issue.4 , pp. 1071-1080
    • Huber, M.D.1    Duquette, M.L.2    Shiels, J.C.3    Maizels, N.4
  • 9
    • 84855829770 scopus 로고    scopus 로고
    • The Werner syndrome protein is distinguished from the Bloom syndrome protein by its capacity to tightly bind diverse DNA structures
    • doi:10.1371/journal.pone.0030189
    • Kamath-Loeb A, Loeb LA, Fry M (2012) The Werner syndrome protein is distinguished from the Bloom syndrome protein by its capacity to tightly bind diverse DNA structures. PLoS One 7(1):e30189. doi:10.1371/journal.pone.0030189
    • (2012) PLoS One , vol.7 , Issue.1
    • Kamath-Loeb, A.1    Loeb, L.A.2    Fry, M.3
  • 10
    • 78649877700 scopus 로고    scopus 로고
    • Structure and function of the regulatory HRDC domain from human Bloom syndrome protein
    • doi:10.1093/nar/gkq586
    • Kim YM, Choi BS (2010) Structure and function of the regulatory HRDC domain from human Bloom syndrome protein. Nucl Acids Res 38(21):7764-7777. doi:10.1093/nar/gkq586
    • (2010) Nucl Acids Res , vol.38 , Issue.21 , pp. 7764-7777
    • Kim, Y.M.1    Choi, B.S.2
  • 11
    • 84888218379 scopus 로고    scopus 로고
    • Structure of the RecQ C-terminal domain of human bloom syndrome protein
    • doi:10.1038/srep03294
    • Kim SY, Hakoshima T, Kitano K (2013) Structure of the RecQ C-terminal domain of human bloom syndrome protein. Sci Rep 3:3294. doi:10.1038/srep03294
    • (2013) Sci Rep , vol.3 , pp. 3294
    • Kim, S.Y.1    Hakoshima, T.2    Kitano, K.3
  • 12
    • 34047267832 scopus 로고    scopus 로고
    • Crystal structure of the HRDC domain of human Werner syndrome protein, WRN
    • DOI 10.1074/jbc.M610142200
    • Kitano K, Yoshihara N, Hakoshima T (2007) Crystal structure of the HRDC domain of human Werner syndrome protein, WRN. J Biol Chem 282(4):2717-2728. doi:10.1074/jbc.M610142200 (Pubitemid 47076758)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.4 , pp. 2717-2728
    • Kitano, K.1    Yoshihara, N.2    Hakoshima, T.3
  • 13
    • 75849122854 scopus 로고    scopus 로고
    • Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN
    • doi:10.1016/j.str.2009.12.011
    • Kitano K, Kim SY, Hakoshima T (2010) Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN. Structure 18(2):177-187. doi:10.1016/j.str.2009.12.011
    • (2010) Structure , vol.18 , Issue.2 , pp. 177-187
    • Kitano, K.1    Kim, S.Y.2    Hakoshima, T.3
  • 14
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14(1):51-55, 29-32
    • (1996) J Mol Graph , vol.14 , Issue.1
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 16
    • 78649467087 scopus 로고    scopus 로고
    • Human RECQ helicases: Roles in DNA metabolism, mutagenesis and cancer biology
    • doi:10.1016/j.semcancer.2010.10.002
    • Monnat RJ Jr (2010) Human RECQ helicases: roles in DNA metabolism, mutagenesis and cancer biology. Semin Cancer Biol 20(5):329-339. doi:10.1016/j.semcancer.2010.10.002
    • (2010) Semin Cancer Biol , vol.20 , Issue.5 , pp. 329-339
    • Monnat Jr., R.J.1
  • 19
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • doi:10.1007/s10858-009-9333-z
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213-223. doi:10.1007/s10858-009-9333-z
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 20
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4(2):171-180
    • (1994) J Biomol NMR , vol.4 , Issue.2 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.