메뉴 건너뛰기




Volumn 294, Issue 5, 1999, Pages 1299-1310

NMR structure of an F-actin-binding 'headpiece' motif from villin

Author keywords

Actin binding protein; Headpiece; NMR structure; Subdomain; Villin

Indexed keywords

ACTIN BINDING PROTEIN; F ACTIN; HISTIDINE; VILLIN;

EID: 0033579417     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3321     Document Type: Article
Times cited : (65)

References (44)
  • 2
    • 0029084382 scopus 로고
    • Isoform cloning, actin-binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily
    • Azim A. C., Knoll J. H., Beggs A. H., Chishti A. H. Isoform cloning, actin-binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily. J. Biol. Chem. 270:1995;17407-17413.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17407-17413
    • Azim, A.C.1    Knoll, J.H.2    Beggs, A.H.3    Chishti, A.H.4
  • 4
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G., Ruben D. J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Letters. 69:1980;185-189.
    • (1980) Chem. Phys. Letters , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 6
    • 0026159281 scopus 로고
    • Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy
    • Clore G. M., Bax A., Gronenborn A. M. Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy. J. Biomol. NMR. 1:1991;13-22.
    • (1991) J. Biomol. NMR , vol.1 , pp. 13-22
    • Clore, G.M.1    Bax, A.2    Gronenborn, A.M.3
  • 7
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F., Grzesiek G., Vuister G., Pfeifer J., Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:1995;227-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 227-293
    • Delaglio, F.1    Grzesiek, G.2    Vuister, G.3    Pfeifer, J.4    Bax, A.5
  • 8
    • 0026507108 scopus 로고
    • Protein immunolocalization in the spread erythrocyte membrane skeleton
    • Derick L. H., Liu S. C., Chishti A. H., Palek J. Protein immunolocalization in the spread erythrocyte membrane skeleton. Eur. J. Cell Biol. 57:1992;317-320.
    • (1992) Eur. J. Cell Biol. , vol.57 , pp. 317-320
    • Derick, L.H.1    Liu, S.C.2    Chishti, A.H.3    Palek, J.4
  • 9
    • 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., Matsudaira P. T. Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin-binding site and structural features of the domain. Biochemistry. 35:1996;12677-12685.
    • (1996) Biochemistry , vol.35 , pp. 12677-12685
    • Doering, D.S.1    Matsudaira, P.T.2
  • 10
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 6:1967;1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 11
    • 0026762463 scopus 로고
    • Expression and localization of villin, fimbrin, and myosin I in differentiating mouse F9 teratocarcinoma cells
    • Ezzell R. M., Leung J., Collins K., Chafel M. M., Cardozo T. J., Matsudaira P. T. Expression and localization of villin, fimbrin, and myosin I in differentiating mouse F9 teratocarcinoma cells. Dev. Biol. 151:1992;575-585.
    • (1992) Dev. Biol. , vol.151 , pp. 575-585
    • Ezzell, R.M.1    Leung, J.2    Collins, K.3    Chafel, M.M.4    Cardozo, T.J.5    Matsudaira, P.T.6
  • 12
    • 0025141518 scopus 로고
    • Studies on the solution conformation of human thioredoxin using heteronuclear 15N-1H nuclear magnetic resonance spectroscopy
    • Forman-Kay J. E., Gronenborn A. M., Kay L. E., Wingfield P. T., Clore G. M. Studies on the solution conformation of human thioredoxin using heteronuclear 15N-1H nuclear magnetic resonance spectroscopy. Biochemistry. 29:1990;1566-1572.
    • (1990) Biochemistry , vol.29 , pp. 1566-1572
    • Forman-Kay, J.E.1    Gronenborn, A.M.2    Kay, L.E.3    Wingfield, P.T.4    Clore, G.M.5
  • 13
    • 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., Louvard D. An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell. 70:1992;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
  • 14
    • 0019569461 scopus 로고
    • Calcium control of microfilaments: Uncoupling of the F-actin-severing and -bundling activity of villin by limited proteolysis in vitro
    • Glenney J. R. J., Weber K. Calcium control of microfilaments: uncoupling of the F-actin-severing and -bundling activity of villin by limited proteolysis in vitro. Proc. Natl Acad. Sci. USA. 78:1981;2810-2814.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 2810-2814
    • Glenney, J.R.J.1    Weber, K.2
  • 15
    • 0345311136 scopus 로고
    • Practical aspects of the E. COSY technique. Measurement of scalar spin-spin coupling constants in peptides
    • Griesinger C., Sorensen O. W., Ernst R. R. Practical aspects of the E. COSY technique. Measurement of scalar spin-spin coupling constants in peptides. J. Magn. Reson. 75:1987;474-492.
    • (1987) J. Magn. Reson. , vol.75 , pp. 474-492
    • Griesinger, C.1    Sorensen, O.W.2    Ernst, R.R.3
  • 16
    • 0024282849 scopus 로고
    • Clean TOCSY for 1H spin system identification in macromolecules
    • Griesinger C., Otting G., Wüthrich K., Ernst R. R. Clean TOCSY for 1H spin system identification in macromolecules. J. Am. Chem. Soc. 110:1988;7870-7872.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7870-7872
    • Griesinger, C.1    Otting, G.2    Wüthrich, K.3    Ernst, R.R.4
  • 17
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm L., Sander C. The FSSP database of structurally aligned protein fold families. Nucl. Acids Res. 22:1993;3600-3609.
    • (1993) Nucl. Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 18
    • 0023793618 scopus 로고
    • Abolition of actin-bundling by phosphorylation of human erythrocyte protein 4.9
    • Husain-Chishti A., Levin A., Branton D. Abolition of actin-bundling by phosphorylation of human erythrocyte protein 4.9. Nature. 334:1988;718-721.
    • (1988) Nature , vol.334 , pp. 718-721
    • Husain-Chishti, A.1    Levin, A.2    Branton, D.3
  • 19
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson B., Blevins R. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.1    Blevins, R.2
  • 20
    • 0031439895 scopus 로고    scopus 로고
    • Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse chromosome 19 and human chromosome 10q25, a region frequently deleted in human cancers
    • Kim A. C., Peters L. L., Knoll J. H., Van Huffel C., Ciciotte S. L., Kleyn P. W., Chishti A. H. Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse chromosome 19 and human chromosome 10q25, a region frequently deleted in human cancers. Genomics. 46:1997;291-293.
    • (1997) Genomics , vol.46 , pp. 291-293
    • Kim, A.C.1    Peters, L.L.2    Knoll, J.H.3    Van Huffel, C.4    Ciciotte, S.L.5    Kleyn, P.W.6    Chishti, A.H.7
  • 21
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R., MacArthur M., Moss D., Thornton J. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 23
    • 0029821680 scopus 로고    scopus 로고
    • Mechanisms of apoptosis and its potential role in renal tubular epithelial cell injury
    • Lieberthal W., Levine J. S. Mechanisms of apoptosis and its potential role in renal tubular epithelial cell injury. Am. J. Phys. 271:1996;F477-F488.
    • (1996) Am. J. Phys. , vol.271
    • Lieberthal, W.1    Levine, J.S.2
  • 26
    • 0031058410 scopus 로고    scopus 로고
    • NMR structure of the 35-residue villin headpiece subdomain
    • McKnight C. J., Matsudaira P. T., Kim P. S. NMR structure of the 35-residue villin headpiece subdomain. Nature Struct. Biol. 4:1997;180-184.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 180-184
    • McKnight, C.J.1    Matsudaira, P.T.2    Kim, P.S.3
  • 27
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore D. C., McIntosh L. P., Russell C. B., Anderson D. E., Dahlquist F. W. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177:1989;44-73.
    • (1989) Methods Enzymol. , vol.177 , pp. 44-73
    • Muchmore, D.C.1    McIntosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 28
    • 0024435833 scopus 로고
    • Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling
    • Neri D., Szyperski T., Otting G., Senn H., Wüthrich K. Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. Biochemistry. 28:1989;7510-7516.
    • (1989) Biochemistry , vol.28 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wüthrich, K.5
  • 30
    • 0030831613 scopus 로고    scopus 로고
    • Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily
    • Pestonjamasp K. N., Pope R. K., Wulfkuhle J. D., Luna E. J. Supervillin (p205): a novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. J. Cell Biol. 139:1997;1255-1269.
    • (1997) J. Cell Biol. , vol.139 , pp. 1255-1269
    • Pestonjamasp, K.N.1    Pope, R.K.2    Wulfkuhle, J.D.3    Luna, E.J.4
  • 31
    • 0026951903 scopus 로고
    • Gradient- tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient- tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 32
    • 0028058169 scopus 로고
    • Characterization of the F-actin-binding domains of villin: Classification of F-actin-binding proteins into two groups according to their binding sites on actin
    • Pope B., Way M., Matsudaira P. T., Weeds A. Characterization of the F-actin-binding domains of villin: classification of F-actin-binding proteins into two groups according to their binding sites on actin. FEBS Letters. 338:1994;58-62.
    • (1994) FEBS Letters , vol.338 , pp. 58-62
    • Pope, B.1    Way, M.2    Matsudaira, P.T.3    Weeds, A.4
  • 33
    • 0030882522 scopus 로고    scopus 로고
    • Epithelial cell growth and differentiation. II. Intestinal apoptosis
    • Potten C. S. Epithelial cell growth and differentiation. II. Intestinal apoptosis. Am. J. Physiol. 273:1997;G253-G257.
    • (1997) Am. J. Physiol. , vol.273
    • Potten, C.S.1
  • 34
    • 0030872241 scopus 로고    scopus 로고
    • Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein
    • Roof D. J., Hayes A., Adamian M., Chishti A., Li T. Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein. J. Cell Biol. 138:1997;575-588.
    • (1997) J. Cell Biol. , vol.138 , pp. 575-588
    • Roof, D.J.1    Hayes, A.2    Adamian, M.3    Chishti, A.4    Li, T.5
  • 35
    • 0003840108 scopus 로고    scopus 로고
    • Department of NMR Spectroscopy Bijvoet Center for Biomolecular Research, Utrecht University
    • Rullmann J. A. C. AQUA, Computer Program. 1996;Department of NMR Spectroscopy Bijvoet Center for Biomolecular Research, Utrecht University.
    • (1996) AQUA, Computer Program
    • Rullmann, J.A.C.1
  • 37
    • 0021989328 scopus 로고
    • Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes
    • Siegel D. L., Branton D. Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes. J. Cell Biol. 100:1985;775-785.
    • (1985) J. Cell Biol. , vol.100 , pp. 775-785
    • Siegel, D.L.1    Branton, D.2
  • 39
    • 0033535605 scopus 로고    scopus 로고
    • A unique talin homologue with a headpiece-like domain is required for the multicellular morphogenesis in Dictyostelium
    • Tsujioka M., Machesky L., Cole S., Yahata K., Inouye K. A unique talin homologue with a headpiece-like domain is required for the multicellular morphogenesis in Dictyostelium. Curr. Biol. 9:1999;389-392.
    • (1999) Curr. Biol. , vol.9 , pp. 389-392
    • Tsujioka, M.1    Machesky, L.2    Cole, S.3    Yahata, K.4    Inouye, K.5
  • 40
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 41
    • 12044259775 scopus 로고
    • Quantitative J correlation: A new approach for measuring homonuclear three-bond J(HN Halpha) coupling constants in 15N enriched proteins
    • Vuister G., Bax A. Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HN Halpha) coupling constants in 15N enriched proteins. J. Am. Chem. Soc. 115:1993;7772-7777.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7772-7777
    • Vuister, G.1    Bax, A.2
  • 42
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner G., Braun W., Havel T. F., Schaumann T., Go N., Wüthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196:1987;611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wüthrich, K.6
  • 43
    • 0033525846 scopus 로고    scopus 로고
    • The electrophoretic karyotype of Entamoeba histolytica
    • Willhoeft U., Tannich E. The electrophoretic karyotype of Entamoeba histolytica. Mol. Biochem. Parasitol. 99:1999;41-53.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 41-53
    • Willhoeft, U.1    Tannich, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.