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Volumn 425, Issue 1, 2010, Pages 55-60

An allosteric transition trapped in an intermediate state of a new kinesin-inhibitor complex

Author keywords

Eg5; Kinesin; Mitosis; S trityl L cysteine

Indexed keywords

ALLOSTERIC TRANSITION; ASYMMETRIC UNIT; BINDING POCKETS; BIPOLAR SPINDLES; BOUND STATE; CANCER CHEMOTHERAPY; CLINICAL TRIAL; CONFORMATIONAL CHANGE; DRUG TARGETS; INHIBITOR COMPLEX; INTERMEDIATE STATE; KINESINS; L-CYSTEINE; MOTOR DOMAIN; SPACE GROUPS; STRUCTURAL CHANGE; STRUCTURAL EVIDENCE;

EID: 72449183762     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20091207     Document Type: Article
Times cited : (63)

References (30)
  • 1
    • 0029417238 scopus 로고
    • Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
    • Blangy, A., Lane, H. A., d'Herin, P., Harper, M., Kress, M. and Nigg, E. A. (1995) Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo. Cell 83, 1159-1169
    • (1995) Cell , vol.83 , pp. 1159-1169
    • Blangy, A.1    Lane, H.A.2    d'Herin, P.3    Harper, M.4    Kress, M.5    Nigg, E.A.6
  • 2
    • 0026739078 scopus 로고
    • Mitotic spindle organization by a plus-end-directed microtubule motor
    • Sawin, K. E., LeGuellec, K., Philippe, M. and Mitchison, T. J. (1992) Mitotic spindle organization by a plus-end-directed microtubule motor. Nature 359, 540-543
    • (1992) Nature , vol.359 , pp. 540-543
    • Sawin, K.E.1    LeGuellec, K.2    Philippe, M.3    Mitchison, T.J.4
  • 3
    • 0028168413 scopus 로고
    • A 'slow' homotetrameric kinesin-related motor protein purified from Drosophila embryos
    • Cole, D. G., Saxton, W. M., Sheehan, K. B. and Scholey, J. M. (1994) A 'slow' homotetrameric kinesin-related motor protein purified from Drosophila embryos. J. Biol. Chem. 269, 22913-22916
    • (1994) J. Biol. Chem , vol.269 , pp. 22913-22916
    • Cole, D.G.1    Saxton, W.M.2    Sheehan, K.B.3    Scholey, J.M.4
  • 4
    • 0347928860 scopus 로고    scopus 로고
    • Targeting the kinesin Eg5 to monitor siRNA transfection in mammalian cells
    • Weil, D., Garcon, L., Harper, M., Dumenil, D., Dautry, F. and Kress, M. (2002) Targeting the kinesin Eg5 to monitor siRNA transfection in mammalian cells. Biotechniques 33, 1244-1248
    • (2002) Biotechniques , vol.33 , pp. 1244-1248
    • Weil, D.1    Garcon, L.2    Harper, M.3    Dumenil, D.4    Dautry, F.5    Kress, M.6
  • 5
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer, T. U., Kapoor, T. M., Haggarty, S. J., King, R. W., Schreiber, S. L. and Mitchison, T. J. (1999) Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 286, 971-974
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1    Kapoor, T.M.2    Haggarty, S.J.3    King, R.W.4    Schreiber, S.L.5    Mitchison, T.J.6
  • 7
    • 33745867225 scopus 로고    scopus 로고
    • S -trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression
    • Skoufias, D. A., DeBonis, S., Saoudi, Y., Lebeau, L., Crevel, I., Cross, R., Wade, R. H., Hackney, D. and Kozielski, F. (2006) S -trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression. J. Biol. Chem. 281, 17559-17569
    • (2006) J. Biol. Chem , vol.281 , pp. 17559-17569
    • Skoufias, D.A.1    DeBonis, S.2    Saoudi, Y.3    Lebeau, L.4    Crevel, I.5    Cross, R.6    Wade, R.H.7    Hackney, D.8    Kozielski, F.9
  • 8
    • 0035816597 scopus 로고    scopus 로고
    • Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker
    • Turner, J., Anderson, R., Guo, J., Beraud, C., Fletterick, R. and Sakowicz, R. (2001) Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. J. Biol. Chem. 276, 25496-25502
    • (2001) J. Biol. Chem , vol.276 , pp. 25496-25502
    • Turner, J.1    Anderson, R.2    Guo, J.3    Beraud, C.4    Fletterick, R.5    Sakowicz, R.6
  • 11
    • 26844579689 scopus 로고    scopus 로고
    • The structure of microtubule motor proteins
    • Marx, A., Muller, J. and Mandelkow, E. (2005) The structure of microtubule motor proteins. Adv. Protein Chem. 71, 299-344
    • (2005) Adv. Protein Chem , vol.71 , pp. 299-344
    • Marx, A.1    Muller, J.2    Mandelkow, E.3
  • 12
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull, F. J., Sablin, E. P., Lau, R., Fletterick, R. J. and Vale, R. D. (1996) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380, 550-555
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 13
    • 0036830220 scopus 로고    scopus 로고
    • Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy
    • Sindelar, C. V., Budny, M. J., Rice, S., Naber, N., Fletterick, R. and Cooke, R. (2002) Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy. Nat. Struct. Biol. 9, 844-848
    • (2002) Nat. Struct. Biol , vol.9 , pp. 844-848
    • Sindelar, C.V.1    Budny, M.J.2    Rice, S.3    Naber, N.4    Fletterick, R.5    Cooke, R.6
  • 16
    • 34848842845 scopus 로고    scopus 로고
    • Geometry of nonbonded interactions involving planar groups in proteins
    • Chakrabarti, P. and Bhattacharyya, R. (2007) Geometry of nonbonded interactions involving planar groups in proteins. Prog. Biophys. Mol. Biol. 95, 83-137
    • (2007) Prog. Biophys. Mol. Biol , vol.95 , pp. 83-137
    • Chakrabarti, P.1    Bhattacharyya, R.2
  • 17
    • 5444274954 scopus 로고    scopus 로고
    • Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5
    • Brier, S., Lemaire, D., Debonis, S., Forest, E. and Kozielski, F. (2004) Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5. Biochemistry 43, 13072-13082
    • (2004) Biochemistry , vol.43 , pp. 13072-13082
    • Brier, S.1    Lemaire, D.2    Debonis, S.3    Forest, E.4    Kozielski, F.5
  • 19
    • 34248158214 scopus 로고    scopus 로고
    • Structure of human Eg5 in complex with a new monastrol-based inhibitor bound in the R configuration
    • Garcia-Saez, I., DeBonis, S., Lopez, R., Trucco, F., Rousseau, B., Thuery, P. and Kozielski, F. (2007) Structure of human Eg5 in complex with a new monastrol-based inhibitor bound in the R configuration. J. Biol. Chem. 282, 9740-9747
    • (2007) J. Biol. Chem , vol.282 , pp. 9740-9747
    • Garcia-Saez, I.1    DeBonis, S.2    Lopez, R.3    Trucco, F.4    Rousseau, B.5    Thuery, P.6    Kozielski, F.7
  • 20
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Daresbury Laboratories, Warrington
    • Leslie, A. G. W. (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB Newsletter on Protein Crystallography, No. 26, Daresbury Laboratories, Warrington
    • (1992) Joint CCP4+ESF-EAMCB Newsletter on Protein Crystallography , Issue.26
    • Leslie, A.G.W.1
  • 21
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, N. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
    • Collaborative Computational Project, N. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 283, 283-291
    • (1993) J. Appl. Crystallogr , vol.283 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystal owing to radiation damage
    • Burmeister, W. P. (2000) Structural changes in a cryo-cooled protein crystal owing to radiation damage. Acta Crystallogr. Sect. D Biol. Crystallogr. 56, 328-341
    • (2000) Acta Crystallogr. Sect. D Biol. Crystallogr , vol.56 , pp. 328-341
    • Burmeister, W.P.1
  • 27
    • 0035073965 scopus 로고    scopus 로고
    • Atomic resolution structures of trypsin provide insight into structural radiation damage
    • Leiros, H. K., McSweeney, S. M. and Smalas, A. O. (2001) Atomic resolution structures of trypsin provide insight into structural radiation damage. Acta Crystallogr. Sect. D Biol. Crystallogr. 57, 488-497
    • (2001) Acta Crystallogr. Sect. D Biol. Crystallogr , vol.57 , pp. 488-497
    • Leiros, H.K.1    McSweeney, S.M.2    Smalas, A.O.3
  • 28
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: Robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • Padilla, J. E. and Yeates, T. O. (2003) A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning. Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 1124-1130
    • (2003) Acta Crystallogr. Sect. D Biol. Crystallogr , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 29
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • Yeates, T. O. (1997) Detecting and overcoming crystal twinning. Methods Enzymol. 276, 344-358
    • (1997) Methods Enzymol , vol.276 , pp. 344-358
    • Yeates, T.O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.