메뉴 건너뛰기




Volumn 3, Issue 6, 2006, Pages 125-138

Dynamic allostery of protein alpha helical coiled-coils

Author keywords

Allostery; Biophysics; Coiled coil; Physics; Protein dynamics; Theory

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; MOLECULAR MOTOR;

EID: 33747137334     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2005.0068     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 0004150063 scopus 로고    scopus 로고
    • Cambridge: Cambridge University Press
    • Boal, D. 2002 Mechanics of the cell. Cambridge: Cambridge University Press.
    • (2002) Mechanics of the cell
    • Boal, D.1
  • 2
    • 0037434697 scopus 로고    scopus 로고
    • dynein structure and power stroke
    • doi:10.1038/nature01377
    • Burgess, S. A., Walker, M. L., Sakakibara, H., Knight, P. J. & Oiwa, K. 2003 dynein structure and power stroke. Nature 421, 715-718. (doi:10.1038/nature01377.)
    • (2003) Nature , vol.421 , pp. 715-718
    • Burgess, S.A.1    Walker, M.L.2    Sakakibara, H.3    Knight, P.J.4    Oiwa, K.5
  • 3
    • 1642321108 scopus 로고    scopus 로고
    • The structure of dynein-c by negative stain electron microscopy
    • doi:10. 1016/j.jsb.2003.10.005
    • Burgess, S., Walker, M., Sakakibara, H., Oiwa, K. & Knight, P. 2004a The structure of dynein-c by negative stain electron microscopy. J. Struct. Biol. 146, 205-216. (doi:10. 1016/j.jsb.2003.10.005.)
    • (2004) J. Struct. Biol , vol.146 , pp. 205-216
    • Burgess, S.1    Walker, M.2    Sakakibara, H.3    Oiwa, K.4    Knight, P.5
  • 4
    • 4344620779 scopus 로고    scopus 로고
    • 20046 Use of negative stain and single-particle image processing to explore dynamic properties of flexible macromolecules
    • doi:10.1016/j.jsb.2004.04.004
    • Burgess, S. A., Walker, M. L., Thirumurugan, K., Trinick, J. & Knight, P. J. 20046 Use of negative stain and single-particle image processing to explore dynamic properties of flexible macromolecules. J. Struct. Biol. 147, 247-258. (doi:10.1016/j.jsb.2004.04.004.)
    • J. Struct. Biol , vol.147 , pp. 247-258
    • Burgess, S.A.1    Walker, M.L.2    Thirumurugan, K.3    Trinick, J.4    Knight, P.J.5
  • 5
    • 9244260409 scopus 로고    scopus 로고
    • San Francisco: University of California
    • Case, D. et al. 2004 AMBER 8. San Francisco: University of California.
    • (2004) AMBER 8
    • Case, D.1
  • 6
    • 0021658956 scopus 로고
    • Allostery without conformational change - a plausible model
    • doi:10.1007/BF00276625
    • Cooper, A. & Dryden, D. T. F. 1984 Allostery without conformational change - a plausible model. Eur. Biophys. J. Biophys. Lett. 11, 103-109. (doi:10.1007/BF00276625.)
    • (1984) Eur. Biophys. J. Biophys. Lett , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 7
    • 0031664002 scopus 로고    scopus 로고
    • The role of the dynein stalk in cytoplasmic and flagellar motility
    • doi:10.1007/s002490050157
    • Gee, M. & Vallee, R. 1998 The role of the dynein stalk in cytoplasmic and flagellar motility. Eur. Biophys. J. Biophys. Lett. 27, 466-473. (doi:10.1007/s002490050157.)
    • (1998) Eur. Biophys. J. Biophys. Lett , vol.27 , pp. 466-473
    • Gee, M.1    Vallee, R.2
  • 8
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • doi:10.1038/37663
    • Gee, M., Heuser, J. & Vallee, R. 1997 An extended microtubule-binding structure within the dynein motor domain. Nature 390, 636-639. (doi:10.1038/37663.)
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.1    Heuser, J.2    Vallee, R.3
  • 9
    • 21244479076 scopus 로고    scopus 로고
    • The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk
    • doi:10.1074/jbc.M501636200
    • Gibbons, I., Garbarino, J. E., Tan, C. E., Reck-Peterson, S. L., Vale, R. D. & Carter, A. P. 2005 The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk. J. Biol. Chem. 280, 23 960-23 965. (doi:10.1074/jbc.M501636200.)
    • (2005) J. Biol. Chem , vol.280
    • Gibbons, I.1    Garbarino, J.E.2    Tan, C.E.3    Reck-Peterson, S.L.4    Vale, R.D.5    Carter, A.P.6
  • 10
    • 19544377327 scopus 로고    scopus 로고
    • Coarse-grained model of entropic allostery
    • doi:10.1103/PhysRevLett.93.098104
    • Hawkins, R. J. & McLeish, T. C. B. 2004 Coarse-grained model of entropic allostery. Phys. Rev. Lett. 93, 098104. (doi:10.1103/PhysRevLett.93.098104.)
    • (2004) Phys. Rev. Lett , vol.93 , pp. 098104
    • Hawkins, R.J.1    McLeish, T.C.B.2
  • 11
    • 0024320810 scopus 로고
    • ADP release is rate limiting in steady-state turnover by the dynein adenosinetriphosphatase
    • doi:10.1021/ bi00439a036
    • Holzbaur, E. & Johnson, K. 1989a ADP release is rate limiting in steady-state turnover by the dynein adenosinetriphosphatase. Biochemistry 28, 5577-5585. (doi:10.1021/ bi00439a036.)
    • (1989) Biochemistry , vol.28 , pp. 5577-5585
    • Holzbaur, E.1    Johnson, K.2
  • 12
    • 0024445251 scopus 로고
    • Microtubules accelerate ADP release by dynein
    • doi:10.1021/bi00443a034
    • Holzbaur, E. & Johnson, K. 1989b Microtubules accelerate ADP release by dynein. Biochemistry 28, 7010-7016. (doi:10.1021/bi00443a034.)
    • (1989) Biochemistry , vol.28 , pp. 7010-7016
    • Holzbaur, E.1    Johnson, K.2
  • 13
    • 0021975705 scopus 로고
    • Pathway of the microtubule-dynein ATPase and the structure of dynein: A comparison with actomyosin
    • doi:10.1146/annurev.bb.14.060185.001113
    • Johnson, K. A. 1985 Pathway of the microtubule-dynein ATPase and the structure of dynein: a comparison with actomyosin. Annu. Rev. Biophys. Biophys. Chem. 14, 161-188. (doi:10.1146/annurev.bb.14.060185.001113. )
    • (1985) Annu. Rev. Biophys. Biophys. Chem , vol.14 , pp. 161-188
    • Johnson, K.A.1
  • 14
    • 0001116457 scopus 로고
    • Supercoiling transitions of closed DNA
    • doi:10.1103/PhysRevE.49.2429
    • Jülicher, F. 1994 Supercoiling transitions of closed DNA. Phys. Rev. E 49, 2429-2435. (doi:10.1103/PhysRevE.49.2429.)
    • (1994) Phys. Rev. E , vol.49 , pp. 2429-2435
    • Jülicher, F.1
  • 15
    • 0242585455 scopus 로고    scopus 로고
    • Configurational entropy and cooperativity between ligand binding and dimerization in glycopeptide antibiotics
    • doi:10.1021/ja027780r
    • Jusuf, S., Loll, P. J. & Axelsen, P. H. 2003 Configurational entropy and cooperativity between ligand binding and dimerization in glycopeptide antibiotics. J. Am. Chem. Soc. 125, 3988-3994. (doi:10.1021/ja027780r.)
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 3988-3994
    • Jusuf, S.1    Loll, P.J.2    Axelsen, P.H.3
  • 16
    • 0346220393 scopus 로고    scopus 로고
    • The role of dynamics in allosteric regulation
    • doi:10.1016/j.sbi.2003.10.008
    • Kern, D. & Zuiderweg, E. R. P. 2003 The role of dynamics in allosteric regulation. Curr. Opin. Struct. Biol. 13, 748-757. (doi:10.1016/j.sbi.2003.10.008.)
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.R.P.2
  • 17
    • 4444330119 scopus 로고    scopus 로고
    • Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein
    • doi:10.1021/ bi048985a
    • Kon, T., Nishiura, M., Ohkura, R., Toyoshima, Y. Y. & Sutoh, K. 2004 Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein. Biochemistry 43, 11266-11274. (doi:10.1021/ bi048985a.)
    • (2004) Biochemistry , vol.43 , pp. 11266-11274
    • Kon, T.1    Nishiura, M.2    Ohkura, R.3    Toyoshima, Y.Y.4    Sutoh, K.5
  • 18
    • 0034001336 scopus 로고    scopus 로고
    • Functional elements within the dynein microtubule-binding domain
    • Koonce, M. & Tikhonenko, I. 2000 Functional elements within the dynein microtubule-binding domain. Mol. Biol. Cell 11, 523-529.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 523-529
    • Koonce, M.1    Tikhonenko, I.2
  • 19
    • 0345714919 scopus 로고    scopus 로고
    • Does axonemal dynein push, pull, or oscillate?
    • doi:10.1002/cm.10148
    • Lindemann, C. B. & Hunt, A. J. 2003 Does axonemal dynein push, pull, or oscillate? Cell Motil. Cytoskeleton 56, 237-244. (doi:10.1002/cm.10148.)
    • (2003) Cell Motil. Cytoskeleton , vol.56 , pp. 237-244
    • Lindemann, C.B.1    Hunt, A.J.2
  • 20
    • 37149001327 scopus 로고    scopus 로고
    • DNA under high tension: Overstretching, undertwisting, and relaxation dynamics
    • doi:10.1103/PhysRevE.57.2134
    • Marko, J. F. 1998 DNA under high tension: overstretching, undertwisting, and relaxation dynamics. Phys. Rev. E 57, 2134-2149. (doi:10.1103/PhysRevE.57.2134.)
    • (1998) Phys. Rev. E , vol.57 , pp. 2134-2149
    • Marko, J.F.1
  • 21
    • 3342957252 scopus 로고    scopus 로고
    • dynein and kinesin share an overlapping microtubule-binding site
    • doi:10.1038/sj. emboj.7600240
    • Mizuno, N., Toba, S., Edamatsu, M., Watai-Nishii, J., Hirokawa, N., Toyoshima, Y. Y. & Kikkawa, M. 2004 dynein and kinesin share an overlapping microtubule-binding site. EMBO J. 23, 2459-2467. (doi:10.1038/sj. emboj.7600240.)
    • (2004) EMBO J , vol.23 , pp. 2459-2467
    • Mizuno, N.1    Toba, S.2    Edamatsu, M.3    Watai-Nishii, J.4    Hirokawa, N.5    Toyoshima, Y.Y.6    Kikkawa, M.7
  • 22
    • 0035089503 scopus 로고    scopus 로고
    • Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases
    • doi:10.1016/S0969-2126(00)00557-8
    • Mocz, G. & Gibbons, I. 2001 Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases. Structure (Camb.) 9, 93-103. (doi:10.1016/S0969-2126(00)00557-8.)
    • (2001) Structure (Camb.) , vol.9 , pp. 93-103
    • Mocz, G.1    Gibbons, I.2
  • 23
    • 0032497194 scopus 로고    scopus 로고
    • Entropic elasticity of twist-storing polymers
    • doi:10. 1021/ma971804a
    • Moroz, J. D. & Nelson, P. 1998 Entropic elasticity of twist-storing polymers. Macromolecules 31, 6333-6347. (doi:10. 1021/ma971804a.)
    • (1998) Macromolecules , vol.31 , pp. 6333-6347
    • Moroz, J.D.1    Nelson, P.2
  • 24
    • 0028978047 scopus 로고
    • Computer modelling of the alpha-helical coiled coil: Packing of side-chains in the inner core
    • doi:10.1006/jmbi.1995. 0352
    • Offer, G. & Sessions, R. 1995 Computer modelling of the alpha-helical coiled coil: packing of side-chains in the inner core. J. Mol. Biol. 249, 967-987. (doi:10.1006/jmbi.1995. 0352.)
    • (1995) J. Mol. Biol , vol.249 , pp. 967-987
    • Offer, G.1    Sessions, R.2
  • 25
    • 0022525167 scopus 로고
    • Activation of the dynein adenosinetriphosphatase by microtubules
    • doi:10.1021/bi00350a022
    • Omoto, C. & Johnson, K. 1986 Activation of the dynein adenosinetriphosphatase by microtubules. Biochemistry 25, 419-427. (doi:10.1021/bi00350a022.)
    • (1986) Biochemistry , vol.25 , pp. 419-427
    • Omoto, C.1    Johnson, K.2
  • 26
    • 0021111979 scopus 로고
    • Characterization of the ATP-sensitive binding of Tetrahymena 30 S dynein to bovine brain microtubules
    • Porter, M. & Johnson, K. 1983a Characterization of the ATP-sensitive binding of Tetrahymena 30 S dynein to bovine brain microtubules. J. Biol. Chem. 258, 6575-6581.
    • (1983) J. Biol. Chem , vol.258 , pp. 6575-6581
    • Porter, M.1    Johnson, K.2
  • 27
    • 0021112029 scopus 로고
    • Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex
    • Porter, M. & Johnson, K. 1983b Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex. J. Biol. Chem. 258, 6582-6587.
    • (1983) J. Biol. Chem , vol.258 , pp. 6582-6587
    • Porter, M.1    Johnson, K.2
  • 28
    • 0024449826 scopus 로고
    • dynein structure and function
    • doi:10.1146/annurev. cb.05.110189.001003
    • Porter, M. & Johnson, K. 1989 dynein structure and function. Annu. Rev. Cell Biol. 5, 119-151. (doi:10.1146/annurev. cb.05.110189.001003.)
    • (1989) Annu. Rev. Cell Biol , vol.5 , pp. 119-151
    • Porter, M.1    Johnson, K.2
  • 29
    • 0038002913 scopus 로고    scopus 로고
    • Writhing geometry of open DNA
    • doi:10.1063/ 1.1569905
    • Rossetto, V. & Maggs, A. C. 2003 Writhing geometry of open DNA. J. Chem. Phys. 118, 9864-9874. (doi:10.1063/ 1.1569905.)
    • (2003) J. Chem. Phys , vol.118 , pp. 9864-9874
    • Rossetto, V.1    Maggs, A.C.2
  • 30
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • doi:10.1083/jcb.150.1.F13
    • Vale, R. 2000 AAA proteins. Lords of the ring. J. Cell Biol. 150, F13-F19. (doi:10.1083/jcb.150.1.F13.)
    • (2000) J. Cell Biol , vol.150
    • Vale, R.1
  • 31
    • 0000751914 scopus 로고
    • Self-linking and the gauss integral in higher dimensions
    • White, J. H. 1969 Self-linking and the gauss integral in higher dimensions. Am. J. Math. 91, 693-728.
    • (1969) Am. J. Math , vol.91 , pp. 693-728
    • White, J.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.