메뉴 건너뛰기




Volumn 45, Issue 7, 2006, Pages 2250-2256

Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles

Author keywords

[No Author keywords available]

Indexed keywords

LIPIDS; MICELLES; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOLIPIDS;

EID: 33144479535     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052332s     Document Type: Article
Times cited : (48)

References (48)
  • 1
    • 0842281645 scopus 로고    scopus 로고
    • Critical control points
    • Danial, N. N., and Korsmeyer, S. J. (2004) Cell death: Critical control points, Cell 116, 205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 2
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: Roles in cell survival and oncogenesis
    • Cory, S., Huang, D. C. S., and Adams, J. M. (2003) The Bcl-2 family: Roles in cell survival and oncogenesis, Oncogene 22, 8590-8607.
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.S.2    Adams, J.M.3
  • 3
    • 14944348965 scopus 로고    scopus 로고
    • The role of BH3-only proteins in the immune system
    • Strasser, A. (2005) The role of BH3-only proteins in the immune system, Nat. Rev. Immunol. 5, 189-200.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 189-200
    • Strasser, A.1
  • 6
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana, T., Bouchier-Hayes, L., Chipuk, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., and Newmeyer, D. D. (2005) BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly, Mol. Cell 17, 525-535.
    • (2005) Mol. Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 8
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., and Green, D. R. (2004) Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis, Science 303, 1010-1014.
    • (2004) Science , vol.303 , pp. 1010-1014
    • Chipuk, J.E.1    Kuwana, T.2    Bouchier-Hayes, L.3    Droin, N.M.4    Newmeyer, D.D.5    Schuler, M.6    Green, D.R.7
  • 9
    • 2342553892 scopus 로고    scopus 로고
    • Mitochondrial p53 activates Bak and causes disruption of Bak-Mcl1 complexes
    • Leu, J. I., Dumont, P., Hafey, M., Murthy, M. E., and George, D. L. (2004) Mitochondrial p53 activates Bak and causes disruption of Bak-Mcl1 complexes, Nat. Cell Biol. 6, 443-450.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 443-450
    • Leu, J.I.1    Dumont, P.2    Hafey, M.3    Murthy, M.E.4    George, D.L.5
  • 12
    • 0030822420 scopus 로고    scopus 로고
    • Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family
    • Aritomi, M., Kunishima, N., Inohara, N., Ishibashi, Y., Ohta, S., and Morikawa, K. (1997) Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family, J. Biol. Chem. 272, 27886-27892.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27886-27892
    • Aritomi, M.1    Kunishima, N.2    Inohara, N.3    Ishibashi, Y.4    Ohta, S.5    Morikawa, K.6
  • 14
    • 0344608883 scopus 로고    scopus 로고
    • The structure of Bcl-w reveal a role for the C-terminal residues in modulating biological activity
    • Hinds, M. G., Lackmann, M., Skea, G. L., Harrison, P. J., Huang, D. C. S., and Day, C. L. (2003) The structure of Bcl-w reveal a role for the C-terminal residues in modulating biological activity, EMBO J. 22, 1497-1507.
    • (2003) EMBO J. , vol.22 , pp. 1497-1507
    • Hinds, M.G.1    Lackmann, M.2    Skea, G.L.3    Harrison, P.J.4    Huang, D.C.S.5    Day, C.L.6
  • 17
    • 14244265108 scopus 로고    scopus 로고
    • Solution structure of prosurvival Mcl-1 and characterization of its binding by proapoptotic BH3-only ligands
    • Day, C. L., Chen, L., Richardson, S. J., Harrison, P. J., Huang, D. C. S., and Hinds, M. G. (2005) Solution structure of prosurvival Mcl-1 and characterization of its binding by proapoptotic BH3-only ligands, J. Biol. Chem. 280, 4738-4744.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4738-4744
    • Day, C.L.1    Chen, L.2    Richardson, S.J.3    Harrison, P.J.4    Huang, D.C.S.5    Hinds, M.G.6
  • 18
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • Chou, J. J., Li, H., Salvesen, G. S., Yuan, J., and Wagner, G. (1999) Solution structure of BID, an intracellular amplifier of apoptotic signaling, Cell 96, 615-624.
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 19
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists
    • McDonnell, J. M., Fushman, D., Milliman, C. L., Korsmeyer, S. J., and Cowburn, D. (1999) Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists, Cell 96, 625-634.
    • (1999) Cell , vol.96 , pp. 625-634
    • McDonnell, J.M.1    Fushman, D.2    Milliman, C.L.3    Korsmeyer, S.J.4    Cowburn, D.5
  • 20
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki, M., Youle, R. J., and Tjandra, N. (2000) Structure of Bax: Coregulation of dimer formation and intracellular localization, Cell 103, 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 23
    • 0042220409 scopus 로고    scopus 로고
    • The structure of a Bcl-xL/Bim fragment complex: Implications for Bim function
    • Liu, X., Dai, S., Zhu, Y., Marrack, P., and Kapper, J. W. (2003) The structure of a Bcl-xL/Bim fragment complex: Implications for Bim function, Immunity 19, 341-352.
    • (2003) Immunity , vol.19 , pp. 341-352
    • Liu, X.1    Dai, S.2    Zhu, Y.3    Marrack, P.4    Kapper, J.W.5
  • 25
    • 0842264375 scopus 로고    scopus 로고
    • Structural studies of apoptosis and ion transport regulatory proteins in membranes
    • Franzin, C. M., Choi, J., Zhai, D., Reed, J. C., and Marassi, F. M. (2004) Structural studies of apoptosis and ion transport regulatory proteins in membranes, Magn. Reson. Chem. 42, 172-179.
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 172-179
    • Franzin, C.M.1    Choi, J.2    Zhai, D.3    Reed, J.C.4    Marassi, F.M.5
  • 27
    • 0031555482 scopus 로고    scopus 로고
    • Three-dimensional structures of proteins involved in programmed cell death
    • Liang, H., and Fesik, S. W. (1997) Three-dimensional structures of proteins involved in programmed cell death, J. Mol. Biol. 274, 291-302.
    • (1997) J. Mol. Biol. , vol.274 , pp. 291-302
    • Liang, H.1    Fesik, S.W.2
  • 28
    • 12844266796 scopus 로고    scopus 로고
    • Conformational changes in BID, a proapoptotic BCL-2 family member, upon membrane binding
    • Oh, K. J., Barbuto, S., Meyer, N., Kim, R. S., Collier, J., and Korsmeyer, S. J. (2005) Conformational changes in BID, a proapoptotic BCL-2 family member, upon membrane binding, J. Biol. Chem. 280, 753-767.
    • (2005) J. Biol. Chem. , vol.280 , pp. 753-767
    • Oh, K.J.1    Barbuto, S.2    Meyer, N.3    Kim, R.S.4    Collier, J.5    Korsmeyer, S.J.6
  • 29
    • 2442551481 scopus 로고    scopus 로고
    • During apoptosis Bcl-2 changes membrane topology at both endoplasmic reticulum and mitochondria
    • Kim, P. K., Annis, M. G., Dlugosz, P. J., Leber, B., and Andrews, D. W. (2004) During apoptosis Bcl-2 changes membrane topology at both endoplasmic reticulum and mitochondria, Mol. Cell 14, 523-529.
    • (2004) Mol. Cell , vol.14 , pp. 523-529
    • Kim, P.K.1    Annis, M.G.2    Dlugosz, P.J.3    Leber, B.4    Andrews, D.W.5
  • 36
    • 0028674384 scopus 로고
    • Investigation of protein motions via relaxation measurements
    • Peng, J. W., and Wagner, G. (1994) Investigation of protein motions via relaxation measurements, Methods Enzymol. 239, 563-596.
    • (1994) Methods Enzymol. , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 37
    • 0029400480 scopus 로고
    • NMRpipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRpipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 38
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T. H., Billeter, M., Guntert, P., and Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR 5, 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Guntert, P.4    Wüthrich, K.5
  • 39
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Domingues, C., Boelens, R., and Bonvin, A. M. J. J. (2003) HADDOCK: A protein-protein docking approach based on biochemical or biophysical information, J. Am. Chem. Soc. 125, 1731-1737.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Domingues, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 41
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A progam for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A progam for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 42
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993) Protein structure comparison by alignment of distance matrices, J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 43
    • 0037138678 scopus 로고    scopus 로고
    • A novel approach for characterizing protein ligand complexes: Molecular basis for specificity of small-molecule Bcl-2 inhibitors
    • Lugovskoy, A. A., Degterev, A. I., Fahmy, A. F., Zhou, P., Gross, J. D., Yuan, J., and Wagner, G. (2002) A novel approach for characterizing protein ligand complexes: Molecular basis for specificity of small-molecule Bcl-2 inhibitors, J. Am. Chem. Soc. 124, 1234-1240.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1234-1240
    • Lugovskoy, A.A.1    Degterev, A.I.2    Fahmy, A.F.3    Zhou, P.4    Gross, J.D.5    Yuan, J.6    Wagner, G.7
  • 44
    • 0141569444 scopus 로고    scopus 로고
    • Discovery, characterization, and structure-activity relationships studies of proapoptotic polyphenol targeting B-cell lymphocyte/leukemia-2 proteins
    • Kitada, S., Leone, M., Sareth, S., Zhai, D., Reed, J. C., and Pellecchia, M. (2003) Discovery, characterization, and structure-activity relationships studies of proapoptotic polyphenol targeting B-cell lymphocyte/leukemia-2 proteins, J. Med. Chem. 46, 4259-4264.
    • (2003) J. Med. Chem. , vol.46 , pp. 4259-4264
    • Kitada, S.1    Leone, M.2    Sareth, S.3    Zhai, D.4    Reed, J.C.5    Pellecchia, M.6
  • 45
    • 17644365389 scopus 로고    scopus 로고
    • Terephthalamide derivatives as mimetics of helical peptides: Disruption of the Bcl-x(L)/Bak interaction
    • Yin, H., Lee, G. I., Sedey, K. A., Rodriguez, J. M., Wang, H. G., Sebti, S. M., and Hamilton, A. D. (2005) Terephthalamide derivatives as mimetics of helical peptides: Disruption of the Bcl-x(L)/Bak interaction, J. Am. Chem. Soc. 127, 5463-5468.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5463-5468
    • Yin, H.1    Lee, G.I.2    Sedey, K.A.3    Rodriguez, J.M.4    Wang, H.G.5    Sebti, S.M.6    Hamilton, A.D.7
  • 47
    • 21844464054 scopus 로고    scopus 로고
    • Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis
    • Annis, M. G., Soucie, B. L., Dlugosz, P. J., Cruz-Aguado, A., Penn, L. Z., Leber, B., and Andrews, D. W. (2005) Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis, EMBO J. 24, 2096-2103.
    • (2005) EMBO J. , vol.24 , pp. 2096-2103
    • Annis, M.G.1    Soucie, B.L.2    Dlugosz, P.J.3    Cruz-Aguado, A.4    Penn, L.Z.5    Leber, B.6    Andrews, D.W.7
  • 48
    • 2942625430 scopus 로고    scopus 로고
    • Bcl-xL sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers
    • Jeong, S. Y., Gaume, B., Lee, Y. J., Hsu, Y. T., Ryu, S. W., Yoon, S. H., and Youle, R. J. (2004) Bcl-xL sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers, EMBO J. 23, 2146-2155.
    • (2004) EMBO J. , vol.23 , pp. 2146-2155
    • Jeong, S.Y.1    Gaume, B.2    Lee, Y.J.3    Hsu, Y.T.4    Ryu, S.W.5    Yoon, S.H.6    Youle, R.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.