메뉴 건너뛰기




Volumn 44, Issue 36, 2005, Pages 11963-11973

High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CYTOLOGY; PROTEINS; STABILITY;

EID: 24644519821     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050850x     Document Type: Article
Times cited : (50)

References (39)
  • 2
    • 0019821604 scopus 로고
    • Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization
    • Glenney, J. R. J., Geisler, N., Kaulfus, P., and Weber, K. (1981) Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization, J. Biol. Chem. 256, 8156-8161.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8156-8161
    • Glenney, J.R.J.1    Geisler, N.2    Kaulfus, P.3    Weber, K.4
  • 3
    • 0018869290 scopus 로고
    • Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner
    • Bretscher, A., and Weber, K. (1980) Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner, Cell 20, 839-847.
    • (1980) Cell , vol.20 , pp. 839-847
    • Bretscher, A.1    Weber, K.2
  • 4
    • 0031984186 scopus 로고    scopus 로고
    • Targeted disruption of the mouse villin gene does not impair the morphogenesis of microvilli
    • Pinson, K. I., Dunbar, L., Samuelson, L., and Gumucio, D. L. (1998) Targeted disruption of the mouse villin gene does not impair the morphogenesis of microvilli, Dev. Dyn. 211, 109-121.
    • (1998) Dev. Dyn. , vol.211 , pp. 109-121
    • Pinson, K.I.1    Dunbar, L.2    Samuelson, L.3    Gumucio, D.L.4
  • 6
    • 1642576026 scopus 로고    scopus 로고
    • Association of villin with phosphatidylinositol 4,5-bisphosphate regulates the actin cytoskeleton
    • Kumar, N., Zhao, P., Tomar, A., Galea, C. A., and Khurana, S. (2004) Association of villin with phosphatidylinositol 4,5-bisphosphate regulates the actin cytoskeleton, J. Biol. Chem. 279, 3096-3110.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3096-3110
    • Kumar, N.1    Zhao, P.2    Tomar, A.3    Galea, C.A.4    Khurana, S.5
  • 7
    • 0033579417 scopus 로고    scopus 로고
    • NMR structure of an F-actin binding "headpiece" motif from villin
    • Vardar, D., Buckley, D., Frank, B., and McKnight, C. (1999) NMR structure of an F-actin binding "headpiece" motif from villin, J. Mol. Biol. 249, 1299-1310.
    • (1999) J. Mol. Biol. , vol.249 , pp. 1299-1310
    • Vardar, D.1    Buckley, D.2    Frank, B.3    McKnight, C.4
  • 8
    • 0031058410 scopus 로고    scopus 로고
    • NMR structure of the 35-residue villin headpiece subdomain
    • McKnight, C. J., Matsudaira, P. T., and Kim, P. S. (1997) NMR structure of the 35-residue villin headpiece subdomain, Nat. Struct. Biol. 4, 180-184.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 180-184
    • McKnight, C.J.1    Matsudaira, P.T.2    Kim, P.S.3
  • 9
    • 0035857402 scopus 로고    scopus 로고
    • 2.1 and 1.8 Å average C-α rmsd structure predictions on two small proteins, HP-36 and S15
    • Lee, M. R., Baker, D., and Kollman, P. A. (2001) 2.1 and 1.8 Å average C-α rmsd structure predictions on two small proteins, HP-36 and S15, J. Am. Chem. Soc. 123, 1040-1046.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1040-1046
    • Lee, M.R.1    Baker, D.2    Kollman, P.A.3
  • 10
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1 μs simulation in aqueous solution
    • Duan, Y., and Kollman, P. (1998) Pathways to a protein folding intermediate observed in a 1 μs simulation in aqueous solution, Science 282, 740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.2
  • 11
    • 0037426218 scopus 로고    scopus 로고
    • Correlation between rate of folding, energy landscape, and topology in the folding of a model protein HP-36
    • Mukherjee, A., and Bagchi, B. (2003) Correlation between rate of folding, energy landscape, and topology in the folding of a model protein HP-36, J. Chem. Phys. 118, 4733-4747.
    • (2003) J. Chem. Phys. , vol.118 , pp. 4733-4747
    • Mukherjee, A.1    Bagchi, B.2
  • 13
    • 0036307683 scopus 로고    scopus 로고
    • Application of the diffusion-collision model to the folding of three-helix bundle proteins
    • Islam, S. A., Karplus, M., and Weaver, D. L. (2002) Application of the diffusion-collision model to the folding of three-helix bundle proteins, J. Mol. Biol. 318, 199-215.
    • (2002) J. Mol. Biol. , vol.318 , pp. 199-215
    • Islam, S.A.1    Karplus, M.2    Weaver, D.L.3
  • 14
    • 0036428782 scopus 로고    scopus 로고
    • Simulation of folding of a small α-helical protein in atomistic detail using worldwide-distributed computine
    • Zagrovic, B., Snow, C. D., Shirts, M. R., and Pande, V. S. (2002) Simulation of folding of a small α-helical protein in atomistic detail using worldwide-distributed computine, J. Mol. Biol. 323, 927-937.
    • (2002) J. Mol. Biol. , vol.323 , pp. 927-937
    • Zagrovic, B.1    Snow, C.D.2    Shirts, M.R.3    Pande, V.S.4
  • 15
    • 0036137805 scopus 로고    scopus 로고
    • Exploratory studies of ab initio protein structure prediction: Multiple copy simulated annealing, AMBER energy functions, and a generalized born/solvent accessibility solvation model
    • Liu, Y. X., and Beveridge, D. L. (2002) Exploratory studies of ab initio protein structure prediction: Multiple copy simulated annealing, AMBER energy functions, and a generalized born/solvent accessibility solvation model, Proteins: Struct., Funct., Genet. 46, 128-146.
    • (2002) Proteins: Struct., Funct., Genet. , vol.46 , pp. 128-146
    • Liu, Y.X.1    Beveridge, D.L.2
  • 16
    • 0037188018 scopus 로고    scopus 로고
    • Protein folding as biased conformational diffusion
    • Sullivan, D. C., and Kuntz, I. D. (2002) Protein folding as biased conformational diffusion, J. Phys. Chem. B 106, 3255-3262.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3255-3262
    • Sullivan, D.C.1    Kuntz, I.D.2
  • 18
    • 0026773096 scopus 로고
    • An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
    • Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J., and Louvard, D. (1992) An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin, Cell 70, 81-92.
    • (1992) Cell , vol.70 , pp. 81-92
    • Friederich, E.1    Vancompernolle, K.2    Huet, C.3    Goethals, M.4    Finidori, J.5    Vandekerckhove, J.6    Louvard, D.7
  • 19
    • 0029843044 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain
    • Doering, D. S., and Matsudaira, P. T. (1996) Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain, Biochemistry 35, 12677-12685.
    • (1996) Biochemistry , vol.35 , pp. 12677-12685
    • Doering, D.S.1    Matsudaira, P.T.2
  • 20
    • 0037931791 scopus 로고    scopus 로고
    • A phage display-based method for determination of relative affinities of mutants. Application of the actin-binding motifs in thymosin β 4 and the villin headpiece
    • Rossenu, S., Leyman, S., Dewitte, D., Peelaers, D., Jonckheere, V., van Troys, M., Vandekerckhove, J., and Ampe, C. (2003) A phage display-based method for determination of relative affinities of mutants. Application of the actin-binding motifs in thymosin β 4 and the villin headpiece, J. Biol. Chem. 278, 16642-16650.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16642-16650
    • Rossenu, S.1    Leyman, S.2    Dewitte, D.3    Peelaers, D.4    Jonckheere, V.5    Van Troys, M.6    Vandekerckhove, J.7    Ampe, C.8
  • 21
  • 22
    • 24644523139 scopus 로고    scopus 로고
    • The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site
    • Frank, B. S., Vardar, D., Chishti, A. H., and McKnight, C. J. (2003) The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site, J. Biol. Chem. 2, 2.
    • (2003) J. Biol. Chem. , vol.2 , pp. 2
    • Frank, B.S.1    Vardar, D.2    Chishti, A.H.3    McKnight, C.J.4
  • 23
    • 0036180616 scopus 로고    scopus 로고
    • The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain
    • Frank, B. S., Vardar, D., Buckley, D. A., and McKnight, C. J. (2002) The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain, Protein Sci. 11, 680-687.
    • (2002) Protein Sci. , vol.11 , pp. 680-687
    • Frank, B.S.1    Vardar, D.2    Buckley, D.A.3    McKnight, C.J.4
  • 24
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D., and Spudich, J. A. (1982) Purification of muscle actin, Methods Enzymol. 85, 164-181.
    • (1982) Methods Enzymol. , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 25
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 26
    • 0033612365 scopus 로고    scopus 로고
    • Anomalous signal of solvent bromides used for phasing of lysozyme
    • Dauter, Z., and Dauter, M. (1999) Anomalous signal of solvent bromides used for phasing of lysozyme, J. Mol. Biol. 289, 93-101.
    • (1999) J. Mol. Biol. , vol.289 , pp. 93-101
    • Dauter, Z.1    Dauter, M.2
  • 31
    • 0028058169 scopus 로고
    • Characterization of the F-actin binding domains of villin: Classification of F-actin binding proteins in to two groups according to their binding sites on actin
    • Pope, B., Way, M., Matsudaira, P. T., and Weeds, A. (1994) Characterization of the F-actin binding domains of villin: Classification of F-actin binding proteins in to two groups according to their binding sites on actin, FEBS Lett. 338, 58-62.
    • (1994) FEBS Lett. , vol.338 , pp. 58-62
    • Pope, B.1    Way, M.2    Matsudaira, P.T.3    Weeds, A.4
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 34
    • 0029012098 scopus 로고
    • Interpretation of binding curves obtained with high receptor concentrations-Practical aid for computer analysis
    • Swillens, S. (1995) Interpretation of binding curves obtained with high receptor concentrations-Practical aid for computer analysis, Mol. Pharm. 47, 1197-1203.
    • (1995) Mol. Pharm. , vol.47 , pp. 1197-1203
    • Swillens, S.1
  • 35
    • 0008501653 scopus 로고    scopus 로고
    • A thermostable 35-residue subdornain within villin headpiece
    • McKnight, C. J., Doering, D. S., Matsudaira, P. T., and Kim, P. S. (1996) A thermostable 35-residue subdornain within villin headpiece, J. Mol. Biol. 260, 126-134.
    • (1996) J. Mol. Biol. , vol.260 , pp. 126-134
    • McKnight, C.J.1    Doering, D.S.2    Matsudaira, P.T.3    Kim, P.S.4
  • 36
    • 0038288925 scopus 로고    scopus 로고
    • Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale: Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein
    • Wang, M., Tang, Y., Sato, S., Vugmeyster, L., McKnight, C. J., Raleigh, D. P., Trott, O., and Palmer, A. G., III (2003) Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale: Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein, J. Am. Chem. Soc. 125, 6032-6033.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6032-6033
    • Wang, M.1    Tang, Y.2    Sato, S.3    Vugmeyster, L.4    McKnight, C.J.5    Raleigh, D.P.6    Trott, O.7    Palmer III, A.G.8
  • 37
    • 0038054301 scopus 로고    scopus 로고
    • Experimental tests of villin subdomain folding simulations
    • Kubelka, J., Eaton, W. A., and Hofrichter, J. (2003) Experimental tests of villin subdomain folding simulations, J. Mol. Biol. 329, 625-630.
    • (2003) J. Mol. Biol. , vol.329 , pp. 625-630
    • Kubelka, J.1    Eaton, W.A.2    Hofrichter, J.3
  • 38
    • 0036307907 scopus 로고    scopus 로고
    • Temperature-dependemt dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein
    • Vugmeyster, L., Trott, O., McKnight, C. J., Raleigh, D. P., and Palmer, A. G., III (2002) Temperature-dependemt dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein, J. Mol. Biol. 320, 841-854.
    • (2002) J. Mol. Biol. , vol.320 , pp. 841-854
    • Vugmeyster, L.1    Trott, O.2    McKnight, C.J.3    Raleigh, D.P.4    Palmer III, A.G.5
  • 39
    • 24644487559 scopus 로고    scopus 로고
    • Infrared T-jump investigation of the folding kinetics of the villin headpiece subdomain
    • Brewer, S. H., Tang, Y. F., Raleigh, D. P., Vu, D. M., Dyer, R. B., and Franzen, S. (2004) Infrared T-jump investigation of the folding kinetics of the villin headpiece subdomain, Biophys. J. 86, 497a-497a.
    • (2004) Biophys. J. , vol.86
    • Brewer, S.H.1    Tang, Y.F.2    Raleigh, D.P.3    Vu, D.M.4    Dyer, R.B.5    Franzen, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.