메뉴 건너뛰기




Volumn 18, Issue 8, 2010, Pages 955-965

Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4

Author keywords

Proteins

Indexed keywords

PROTEIN E4B; PROTEIN UFD2A; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 77955493101     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2010.04.017     Document Type: Article
Times cited : (43)

References (52)
  • 3
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger-a common domain in ubiquitination
    • Aravind L., Koonin E.V. The U box is a modified RING finger-a common domain in ubiquitination. Curr. Biol. 2000, 10:R132-R134.
    • (2000) Curr. Biol. , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 4
    • 3142608985 scopus 로고    scopus 로고
    • Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains
    • Botuyan M.V., Nominé Y., Yu X., Juranić N., Macura S., Chen J., Mer G. Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. Structure 2004, 12:1137-1146.
    • (2004) Structure , vol.12 , pp. 1137-1146
    • Botuyan, M.V.1    Nominé, Y.2    Yu, X.3    Juranić, N.4    Macura, S.5    Chen, J.6    Mer, G.7
  • 5
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • Brzovic P.S., Lissounov A., Christensen D.E., Hoyt D.W., Klevit R.E. A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol. Cell 2006, 21:873-880.
    • (2006) Mol. Cell , vol.21 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 6
    • 0035692486 scopus 로고    scopus 로고
    • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles
    • Chou J.J., Gaemers S., Howder B., Louis J.M., Bax A. A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. J. Biomol. NMR 2001, 21:377-382.
    • (2001) J. Biomol. NMR , vol.21 , pp. 377-382
    • Chou, J.J.1    Gaemers, S.2    Howder, B.3    Louis, J.M.4    Bax, A.5
  • 8
    • 0033057676 scopus 로고    scopus 로고
    • A doublet-separated sensitivity-enhanced HSQC for the determination of scalar and dipolar one-bond J-couplings
    • Cordier F., Dingley A.J., Grzesiek S. A doublet-separated sensitivity-enhanced HSQC for the determination of scalar and dipolar one-bond J-couplings. J. Biomol. NMR 1999, 13:175-180.
    • (1999) J. Biomol. NMR , vol.13 , pp. 175-180
    • Cordier, F.1    Dingley, A.J.2    Grzesiek, S.3
  • 10
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 1999, 13:289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 13
    • 1842607157 scopus 로고    scopus 로고
    • Structural model of the UbcH5b/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches
    • Dominguez C., Bonvin A.M., Winkler G.S., van Schaik F.M., Timmers H.T., Boelens R. Structural model of the UbcH5b/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches. Structure 2004, 12:633-644.
    • (2004) Structure , vol.12 , pp. 633-644
    • Dominguez, C.1    Bonvin, A.M.2    Winkler, G.S.3    van Schaik, F.M.4    Timmers, H.T.5    Boelens, R.6
  • 16
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: a multifaceted approach to macromolecular structure
    • Ferentz A.E., Wagner G. NMR spectroscopy: a multifaceted approach to macromolecular structure. Q. Rev. Biophys. 2000, 33:29-65.
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 17
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert P. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 2004, 278:353-378.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 19
    • 3042856481 scopus 로고    scopus 로고
    • Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones
    • Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I. Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones. Genes Cells 2004, 9:533-548.
    • (2004) Genes Cells , vol.9 , pp. 533-548
    • Hatakeyama, S.1    Matsumoto, M.2    Yada, M.3    Nakayama, K.I.4
  • 21
    • 0029588670 scopus 로고
    • Identification of a family of closely related human ubiquitin conjugating enzymes
    • Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M. Identification of a family of closely related human ubiquitin conjugating enzymes. J. Biol. Chem. 1995, 270:30408-30414.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30408-30414
    • Jensen, J.P.1    Bates, P.W.2    Yang, M.3    Vierstra, R.D.4    Weissman, A.M.5
  • 22
    • 34249765651 scopus 로고
    • NMRView: a computer program for the visualization and analysis of NMR data
    • Johnson B.A., Blevins R.A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4:603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 23
    • 0034795293 scopus 로고    scopus 로고
    • NC' coupling constants in the hydrogen-bonding network of human ubiquitin
    • NC' coupling constants in the hydrogen-bonding network of human ubiquitin. J. Am. Chem. Soc. 2001, 123:4099-4100.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4099-4100
    • Juranić, N.1    Macura, S.2
  • 26
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H.D., Mayer T.U., Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999, 96:635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 27
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • 29-32
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 1996, 14:51-55. 29-32.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 28
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Herrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Herrick, K.2
  • 29
    • 27144526164 scopus 로고    scopus 로고
    • Orchestra for assembly and fate of polyubiquitin chains
    • Kuhlbrodt K., Mouysset J., Hoppe T. Orchestra for assembly and fate of polyubiquitin chains. Essays Biochem. 2005, 41:1-14.
    • (2005) Essays Biochem. , vol.41 , pp. 1-14
    • Kuhlbrodt, K.1    Mouysset, J.2    Hoppe, T.3
  • 30
    • 33747858757 scopus 로고    scopus 로고
    • NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis
    • Lindahl E., Azuara C., Koehl P., Delarue M. NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis. Nucleic Acids Res. 2006, 34:W52-W56.
    • (2006) Nucleic Acids Res. , vol.34
    • Lindahl, E.1    Azuara, C.2    Koehl, P.3    Delarue, M.4
  • 36
    • 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. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 30044437590 scopus 로고    scopus 로고
    • Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases
    • Ozkan E., Yu H., Deisenhofer J. Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Proc. Natl. Acad. Sci. USA 2005, 102:18890-18895.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18890-18895
    • Ozkan, E.1    Yu, H.2    Deisenhofer, J.3
  • 38
    • 2542579359 scopus 로고    scopus 로고
    • Getting into position: the catalytic mechanisms of protein ubiquitylation
    • Passmore L.A., Barford D. Getting into position: the catalytic mechanisms of protein ubiquitylation. Biochem. J. 2004, 379:513-525.
    • (2004) Biochem. J. , vol.379 , pp. 513-525
    • Passmore, L.A.1    Barford, D.2
  • 39
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 2001, 70:503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 40
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: structures, functions, mechanisms
    • Pickart C.M., Eddins M.J. Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 2004, 1695:55-72.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 41
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H., Rape M., Braun S., Rumpf S., Hoege C., Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 2005, 120:73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 43
    • 35649014889 scopus 로고    scopus 로고
    • Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p
    • Tu D., Li W., Ye Y., Brunger A.T. Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p. Proc. Natl. Acad. Sci. USA 2007, 104:15599-15606.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 15599-15606
    • Tu, D.1    Li, W.2    Ye, Y.3    Brunger, A.T.4
  • 44
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: can low affinity systems be studied by isothermal titration calorimetry?
    • Turnbull W.B., Daranas A.H. On the value of c: can low affinity systems be studied by isothermal titration calorimetry?. J. Am. Chem. Soc. 2003, 125:14859-14866.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 45
    • 30144439025 scopus 로고    scopus 로고
    • The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases
    • Vander Kooi C.W., Ohi M.D., Rosenberg J.A., Oldham M.L., Newcomer M.E., Gould K.L., Chazin W.J. The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases. Biochemistry 2006, 45:121-130.
    • (2006) Biochemistry , vol.45 , pp. 121-130
    • Vander Kooi, C.W.1    Ohi, M.D.2    Rosenberg, J.A.3    Oldham, M.L.4    Newcomer, M.E.5    Gould, K.L.6    Chazin, W.J.7
  • 46
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A.M. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2001, 2:169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 47
    • 33645955898 scopus 로고    scopus 로고
    • Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein
    • Xu Z., Devlin K.I., Ford M.G., Nix J.C., Qin J., Misra S. Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein. Biochemistry 2006, 45:4749-4759.
    • (2006) Biochemistry , vol.45 , pp. 4749-4759
    • Xu, Z.1    Devlin, K.I.2    Ford, M.G.3    Nix, J.C.4    Qin, J.5    Misra, S.6
  • 48
    • 44349182079 scopus 로고    scopus 로고
    • Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes
    • Xu Z., Kohli E., Devlin K.I., Bold M., Nix J.C., Misra S. Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes. BMC Struct. Biol. 2008, 8:26.
    • (2008) BMC Struct. Biol. , vol.8 , pp. 26
    • Xu, Z.1    Kohli, E.2    Devlin, K.I.3    Bold, M.4    Nix, J.C.5    Misra, S.6
  • 49
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye Y., Rape M. Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol. 2009, 10:755-764.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 51
    • 27944495299 scopus 로고    scopus 로고
    • Chaperoned ubiquitylation-crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
    • Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H. Chaperoned ubiquitylation-crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. Mol. Cell 2005, 20:525-538.
    • (2005) Mol. Cell , vol.20 , pp. 525-538
    • Zhang, M.1    Windheim, M.2    Roe, S.M.3    Peggie, M.4    Cohen, P.5    Prodromou, C.6    Pearl, L.H.7
  • 52
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N., Wang P., Jeffrey P.D., Pavletich N.P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 2000, 102:533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.