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Volumn 14, Issue 3, 2004, Pages 405-412

Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: Implications for signaling

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; BACH1 PHOSPHOPEPTIDE; BRCA1 PROTEIN; PEPTIDE; PHENYLALANINE; PHOSPHOPEPTIDE; UNCLASSIFIED DRUG;

EID: 2342484423     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00238-2     Document Type: Article
Times cited : (158)

References (38)
  • 1
    • 0031046294 scopus 로고    scopus 로고
    • A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins
    • Bork P., Hofmann K., Bucher P., Neuwald A.F., Altschul S.F., Koonin E.V. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J. 11:1997;68-76
    • (1997) FASEB J. , vol.11 , pp. 68-76
    • Bork, P.1    Hofmann, K.2    Bucher, P.3    Neuwald, A.F.4    Altschul, S.F.5    Koonin, E.V.6
  • 2
    • 0242285628 scopus 로고    scopus 로고
    • Cell signaling. the BRCT domain: Signaling with friends?
    • Caldecott K.W. Cell signaling. The BRCT domain. signaling with friends? Science. 302:2003;579-580
    • (2003) Science , vol.302 , pp. 579-580
    • Caldecott, K.W.1
  • 3
    • 0031031787 scopus 로고    scopus 로고
    • From BRCA1 to RAP1: A widespread BRCT module closely associated with DNA repair
    • Callebaut I., Mornon J.P. From BRCA1 to RAP1. a widespread BRCT module closely associated with DNA repair FEBS Lett. 400:1997;25-30
    • (1997) FEBS Lett. , vol.400 , pp. 25-30
    • Callebaut, I.1    Mornon, J.P.2
  • 4
    • 1442281478 scopus 로고    scopus 로고
    • The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations
    • Cantor S., Drapkin R., Zhang F., Lin Y., Han J., Pamidi S., Livingston D.M. The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. Proc. Natl. Acad. Sci. USA. 101:2004;2357-2362
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2357-2362
    • Cantor, S.1    Drapkin, R.2    Zhang, F.3    Lin, Y.4    Han, J.5    Pamidi, S.6    Livingston, D.M.7
  • 6
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y., Gorina S., Jeffrey P.D., Pavletich N.P. Crystal structure of a p53 tumor suppressor-DNA complex. understanding tumorigenic mutations Science. 265:1994;346-355
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 7
    • 0033527717 scopus 로고    scopus 로고
    • Requirement of ATM-dependent phosphorylation of brca1 in the DNA damage response to double-strand breaks
    • Cortez D., Wang Y., Qin J., Elledge S.J. Requirement of ATM-dependent phosphorylation of brca1 in the DNA damage response to double-strand breaks. Science. 286:1999;1100-1102
    • (1999) Science , vol.286 , pp. 1100-1102
    • Cortez, D.1    Wang, Y.2    Qin, J.3    Elledge, S.J.4
  • 9
    • 0027433563 scopus 로고
    • Genetic linkage analysis in familial breast and ovarian cancer: Results from 214 families. the Breast Cancer Linkage Consortium
    • Easton D.F., Bishop D.T., Ford D., Crockford G.P. Genetic linkage analysis in familial breast and ovarian cancer. results from 214 families. The Breast Cancer Linkage Consortium Am. J. Hum. Genet. 52:1993;678-701
    • (1993) Am. J. Hum. Genet. , vol.52 , pp. 678-701
    • Easton, D.F.1    Bishop, D.T.2    Ford, D.3    Crockford, G.P.4
  • 10
    • 0028034348 scopus 로고
    • Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families
    • Friedman L.S., Ostermeyer E.A., Szabo C.I., Dowd P., Lynch E.D., Rowell S.E., King M.C. Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families. Nat. Genet. 8:1994;399-404
    • (1994) Nat. Genet. , vol.8 , pp. 399-404
    • Friedman, L.S.1    Ostermeyer, E.A.2    Szabo, C.I.3    Dowd, P.4    Lynch, E.D.5    Rowell, S.E.6    King, M.C.7
  • 12
    • 19144367118 scopus 로고    scopus 로고
    • Rapid detection of regionally clustered germ-line BRCA1 mutations by multiplex heteroduplex analysis. UKCCCR Familial Ovarian Cancer Study Group
    • Gayther S.A., Harrington P., Russell P., Kharkevich G., Garkavtseva R.F., Ponder B.A. Rapid detection of regionally clustered germ-line BRCA1 mutations by multiplex heteroduplex analysis. UKCCCR Familial Ovarian Cancer Study Group. Am. J. Hum. Genet. 58:1996;451-456
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 451-456
    • Gayther, S.A.1    Harrington, P.2    Russell, P.3    Kharkevich, G.4    Garkavtseva, R.F.5    Ponder, B.A.6
  • 15
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
  • 17
    • 0030187780 scopus 로고    scopus 로고
    • BRCA1 protein products. Functional motifs
    • Koonin E.V., Altschul S.F., Bork P. BRCA1 protein products. Functional motifs. Nat. Genet. 13:1996;266-268
    • (1996) Nat. Genet. , vol.13 , pp. 266-268
    • Koonin, E.V.1    Altschul, S.F.2    Bork, P.3
  • 18
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 0345352653 scopus 로고    scopus 로고
    • Regulation of E2F1 by BRCT domain-containing protein TopBP1
    • Liu K., Lin F.T., Ruppert J.M., Lin W.C. Regulation of E2F1 by BRCT domain-containing protein TopBP1. Mol. Cell. Biol. 23:2003;3287-3304
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3287-3304
    • Liu, K.1    Lin, F.T.2    Ruppert, J.M.3    Lin, W.C.4
  • 20
    • 0037468232 scopus 로고    scopus 로고
    • MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways
    • Lou Z., Minter-Dykhouse K., Wu X., Chen J. MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways. Nature. 421:2003;957-961
    • (2003) Nature , vol.421 , pp. 957-961
    • Lou, Z.1    Minter-Dykhouse, K.2    Wu, X.3    Chen, J.4
  • 21
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke I.A., Lowery D.M., Nguyen A., Yaffe M.B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science. 302:2003;636-639
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 23
    • 84920325457 scopus 로고
    • AMoRe and automated package for molecular replacement
    • Navaza J. AMoRe and automated package for molecular replacement. Acta Crystallogr. A. 50:1994;157-163
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct Funct Genet. 11:1991;281-296
    • (1991) Proteins: Struct Funct Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0346101743 scopus 로고    scopus 로고
    • Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains
    • Rodriguez M., Yu X., Chen J., Songyang Z. Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains. J. Biol. Chem. 278:2003;52914-52918
    • (2003) J. Biol. Chem. , vol.278 , pp. 52914-52918
    • Rodriguez, M.1    Yu, X.2    Chen, J.3    Songyang, Z.4
  • 27
    • 0034707053 scopus 로고    scopus 로고
    • In search of the tumour-suppressor functions of BRCA1 and BRCA2
    • Scully R., Livingston D.M. In search of the tumour-suppressor functions of BRCA1 and BRCA2. Nature. 408:2000;429-432
    • (2000) Nature , vol.408 , pp. 429-432
    • Scully, R.1    Livingston, D.M.2
  • 28
    • 0030850047 scopus 로고    scopus 로고
    • Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage
    • a
    • Scully R., Chen J., Ochs R.L., Keegan K., Hoekstra M., Feunteun J., Livingston D.M. Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage. Cell. 90:1997;425-435. a
    • (1997) Cell , vol.90 , pp. 425-435
    • Scully, R.1    Chen, J.2    Ochs, R.L.3    Keegan, K.4    Hoekstra, M.5    Feunteun, J.6    Livingston, D.M.7
  • 32
    • 0030499814 scopus 로고    scopus 로고
    • Correlated phasing of multiple isomorphous replacement data
    • Terwilliger T.C., Berendzen J. Correlated phasing of multiple isomorphous replacement data. Acta Crystallogr. D. 52:1996;749-757
    • (1996) Acta Crystallogr. D , vol.52 , pp. 749-757
    • Terwilliger, T.C.1    Berendzen, J.2
  • 33
    • 0035057806 scopus 로고    scopus 로고
    • BRCA1 and BRCA2 and the genetics of breast and ovarian cancer
    • Welcsh P.L., King M.C. BRCA1 and BRCA2 and the genetics of breast and ovarian cancer. Hum. Mol. Genet. 10:2001;605-713
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 605-713
    • Welcsh, P.L.1    King, M.C.2
  • 34
    • 0034809456 scopus 로고    scopus 로고
    • Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1
    • Williams R.S., Green R., Glover J.N. Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1. Nat. Struct. Biol. 8:2001;838-842
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 838-842
    • Williams, R.S.1    Green, R.2    Glover, J.N.3
  • 36
    • 18244362844 scopus 로고    scopus 로고
    • Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling
    • Wu J.W., Hu M., Chai J., Seoane J., Huse M., Li C., Rigotti D.J., Kyin S., Muir T.W., Fairman R., et al. Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling. Mol. Cell. 8:2001;1277-1289
    • (2001) Mol. Cell , vol.8 , pp. 1277-1289
    • Wu, J.W.1    Hu, M.2    Chai, J.3    Seoane, J.4    Huse, M.5    Li, C.6    Rigotti, D.J.7    Kyin, S.8    Muir, T.W.9    Fairman, R.10
  • 37
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • Yaffe M.B., Elia A.E. Phosphoserine/threonine-binding domains. Curr. Opin. Cell Biol. 13:2001;131-138
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 131-138
    • Yaffe, M.B.1    Elia, A.E.2
  • 38
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu X., Chini C.C., He M., Mer G., Chen J. The BRCT domain is a phospho-protein binding domain. Science. 302:2003;639-642
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5


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