메뉴 건너뛰기




Volumn 162, Issue 2, 2008, Pages 229-236

Crystal structure of human transgelin

Author keywords

Actin binding; CH domain; Crystal structure; Transgelin

Indexed keywords

ACTIN; BIOLOGICAL MARKER; CALPONIN; RAS PROTEIN; TRANSGELIN;

EID: 42649116790     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.01.005     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 0024512827 scopus 로고
    • Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene encoding a putative actin-associated protein (p27)
    • Almendral J.M., Santaren J.F., Perera J., Zerial M., and Bravo R. Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene encoding a putative actin-associated protein (p27). Exp. Cell Res. 181 (1989) 518-530
    • (1989) Exp. Cell Res. , vol.181 , pp. 518-530
    • Almendral, J.M.1    Santaren, J.F.2    Perera, J.3    Zerial, M.4    Bravo, R.5
  • 2
    • 0032533444 scopus 로고    scopus 로고
    • Structural comparisons of calponin homology domains: implications for actin binding
    • Banuelos S., Saraste M., and Carugo K.D. Structural comparisons of calponin homology domains: implications for actin binding. Structure 6 (1998) 1419-1431
    • (1998) Structure , vol.6 , pp. 1419-1431
    • Banuelos, S.1    Saraste, M.2    Carugo, K.D.3
  • 3
    • 0036180282 scopus 로고    scopus 로고
    • Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin: calponin
    • Bramham J., Hodgkinson J.L., Smith B.O., Uhrin D., Barlow P.N., and Winder S.J. Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin: calponin. Structure (Camb.) 10 (2002) 249-258
    • (2002) Structure (Camb.) , vol.10 , pp. 249-258
    • Bramham, J.1    Hodgkinson, J.L.2    Smith, B.O.3    Uhrin, D.4    Barlow, P.N.5    Winder, S.J.6
  • 6
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • Castresana J., and Saraste M. Does Vav bind to F-actin through a CH domain?. FEBS Lett. 374 (1995) 149-151
    • (1995) FEBS Lett. , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 7
    • 1842830455 scopus 로고    scopus 로고
    • SM22alpha modulates vascular smooth muscle cell phenotype during atherogenesis
    • Feil S., Hofmann F., and Feil R. SM22alpha modulates vascular smooth muscle cell phenotype during atherogenesis. Circ. Res. 94 (2004) 863-865
    • (2004) Circ. Res. , vol.94 , pp. 863-865
    • Feil, S.1    Hofmann, F.2    Feil, R.3
  • 9
    • 0032563965 scopus 로고    scopus 로고
    • Single calponin homology domains are not actin-binding domains
    • Gimona M., and Winder S.J. Single calponin homology domains are not actin-binding domains. Curr. Biol. 8 (1998) R674-R675
    • (1998) Curr. Biol. , vol.8
    • Gimona, M.1    Winder, S.J.2
  • 10
    • 0031822886 scopus 로고    scopus 로고
    • The single CH domain of calponin is neither sufficient nor necessary for F-actin binding
    • Gimona M., and Mital R. The single CH domain of calponin is neither sufficient nor necessary for F-actin binding. J. Cell Sci. 111 Pt. 13 (1998) 1813-1821
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 13 , pp. 1813-1821
    • Gimona, M.1    Mital, R.2
  • 13
    • 0038107547 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae calponin/transgelin homolog Scp1 functions with fimbrin to regulate stability and organization of the actin cytoskeleton
    • Goodman A., Goode B.L., Matsudaira P., and Fink G.R. The Saccharomyces cerevisiae calponin/transgelin homolog Scp1 functions with fimbrin to regulate stability and organization of the actin cytoskeleton. Mol. Biol. Cell 14 (2003) 2617-2629
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2617-2629
    • Goodman, A.1    Goode, B.L.2    Matsudaira, P.3    Fink, G.R.4
  • 15
    • 0141480958 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)
    • Hayashi I., and Ikura M. Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1). J. Biol. Chem. 278 (2003) 36430-36434
    • (2003) J. Biol. Chem. , vol.278 , pp. 36430-36434
    • Hayashi, I.1    Ikura, M.2
  • 16
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm L., and Sander C. Dali/FSSP classification of three-dimensional protein folds. Nucleic Acids Res. 25 (1997) 231-234
    • (1997) Nucleic Acids Res. , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0030894716 scopus 로고    scopus 로고
    • A serum response factor-dependent transcriptional regulatory program identifies distinct smooth muscle cell sublineages
    • Kim S., Lu M.M., Ip H.S., Parmacek M.S., and Clendenin C. A serum response factor-dependent transcriptional regulatory program identifies distinct smooth muscle cell sublineages. Mol. Cell Biol. 17 (1997) 2266-2278
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2266-2278
    • Kim, S.1    Lu, M.M.2    Ip, H.S.3    Parmacek, M.S.4    Clendenin, C.5
  • 20
    • 0028287673 scopus 로고
    • Purification, characterization, and partial sequence analysis of a new 25-kDa actin-binding protein from bovine aorta: a SM22 homolog
    • Kobayashi R., Kubota T., and Hidaka H. Purification, characterization, and partial sequence analysis of a new 25-kDa actin-binding protein from bovine aorta: a SM22 homolog. Biochem. Biophys. Res. Commun. 198 (1994) 1275-1280
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 1275-1280
    • Kobayashi, R.1    Kubota, T.2    Hidaka, H.3
  • 21
    • 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. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 22
    • 0030781498 scopus 로고    scopus 로고
    • Fibroblast transgelin and smooth muscle SM22alpha are the same protein, the expression of which is down-regulated in many cell lines
    • Lawson D., Harrison M., and Shapland C. Fibroblast transgelin and smooth muscle SM22alpha are the same protein, the expression of which is down-regulated in many cell lines. Cell Motil. Cytoskeleton 38 (1997) 250-257
    • (1997) Cell Motil. Cytoskeleton , vol.38 , pp. 250-257
    • Lawson, D.1    Harrison, M.2    Shapland, C.3
  • 23
    • 0023644595 scopus 로고
    • Isolation and characterization of an abundant and novel 22-kDa protein (SM22) from chicken gizzard smooth muscle
    • Lees-Miller J.P., Heeley D.H., Smillie L.B., and Kay C.M. Isolation and characterization of an abundant and novel 22-kDa protein (SM22) from chicken gizzard smooth muscle. J. Biol. Chem. 262 (1987) 2988-2993
    • (1987) J. Biol. Chem. , vol.262 , pp. 2988-2993
    • Lees-Miller, J.P.1    Heeley, D.H.2    Smillie, L.B.3    Kay, C.M.4
  • 24
    • 0029670963 scopus 로고    scopus 로고
    • SM22 alpha, a marker of adult smooth muscle, is expressed in multiple myogenic lineages during embryogenesis
    • Li L., Miano J.M., Cserjesi P., and Olson E.N. SM22 alpha, a marker of adult smooth muscle, is expressed in multiple myogenic lineages during embryogenesis. Circ. Res. 78 (1996) 188-195
    • (1996) Circ. Res. , vol.78 , pp. 188-195
    • Li, L.1    Miano, J.M.2    Cserjesi, P.3    Olson, E.N.4
  • 25
    • 33846994767 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of transgelin
    • Liao X., Li S., Lou Z., Chen Z., and Bartlam M. Crystallization and preliminary crystallographic analysis of transgelin. Protein Pept. Lett. 14 (2007) 209-211
    • (2007) Protein Pept. Lett. , vol.14 , pp. 209-211
    • Liao, X.1    Li, S.2    Lou, Z.3    Chen, Z.4    Bartlam, M.5
  • 26
    • 0034921574 scopus 로고    scopus 로고
    • Invited review: cross-bridge regulation by thin filament-associated proteins
    • Morgan K.G., and Gangopadhyay S.S. Invited review: cross-bridge regulation by thin filament-associated proteins. J. Appl. Physiol. 91 (2001) 953-962
    • (2001) J. Appl. Physiol. , vol.91 , pp. 953-962
    • Morgan, K.G.1    Gangopadhyay, S.S.2
  • 27
    • 0034657791 scopus 로고    scopus 로고
    • The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy
    • Norwood F.L., Sutherland-Smith A.J., Keep N.H., and Kendrick-Jones J. The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. Struct. Fold Des. 8 (2000) 481-491
    • (2000) Struct. Fold Des. , vol.8 , pp. 481-491
    • Norwood, F.L.1    Sutherland-Smith, A.J.2    Keep, N.H.3    Kendrick-Jones, J.4
  • 28
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily
    • Olski T.M., Noegel A.A., and Korenbaum E. Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily. J. Cell Sci. 114 (2001) 525-538
    • (2001) J. Cell Sci. , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter Jr. C.W., and Sweet R.M. (Eds), Academic Press, New York
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter Jr. C.W., and Sweet R.M. (Eds). Macromolecular Crystallography, Part A (1997), Academic Press, New York 307-326
    • (1997) Macromolecular Crystallography, Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0028306815 scopus 로고
    • Cloning and sequencing of cDNAs encoding the actin cross-linking protein transgelin defines a new family of actin-associated proteins
    • Prinjha R.K., Shapland C.E., Hsuan J.J., Totty N.F., Mason I.J., and Lawson D. Cloning and sequencing of cDNAs encoding the actin cross-linking protein transgelin defines a new family of actin-associated proteins. Cell Motil. Cytoskeleton 28 (1994) 243-255
    • (1994) Cell Motil. Cytoskeleton , vol.28 , pp. 243-255
    • Prinjha, R.K.1    Shapland, C.E.2    Hsuan, J.J.3    Totty, N.F.4    Mason, I.J.5    Lawson, D.6
  • 31
    • 0027252650 scopus 로고
    • Purification and properties of transgelin: a transformation and shape change sensitive actin-gelling protein
    • Shapland C., Hsuan J.J., Totty N.F., and Lawson D. Purification and properties of transgelin: a transformation and shape change sensitive actin-gelling protein. J. Cell Biol. 121 (1993) 1065-1073
    • (1993) J. Cell Biol. , vol.121 , pp. 1065-1073
    • Shapland, C.1    Hsuan, J.J.2    Totty, N.F.3    Lawson, D.4
  • 32
    • 0037155896 scopus 로고    scopus 로고
    • Loss of transgelin in breast and colon tumors and in RIE-1 cells by Ras deregulation of gene expression through Raf-independent pathways
    • Shields J.M., Rogers-Graham K., and Der C.J. Loss of transgelin in breast and colon tumors and in RIE-1 cells by Ras deregulation of gene expression through Raf-independent pathways. J. Biol. Chem. 277 (2002) 9790-9799
    • (2002) J. Biol. Chem. , vol.277 , pp. 9790-9799
    • Shields, J.M.1    Rogers-Graham, K.2    Der, C.J.3
  • 35
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 36
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 0026779315 scopus 로고
    • A novel gene encoding a smooth muscle protein is overexpressed in senescent human fibroblasts
    • Thweatt R., Lumpkin C.K., and Goldstein S. A novel gene encoding a smooth muscle protein is overexpressed in senescent human fibroblasts. Biochem. Biophys. Res. Commun. 187 (1992) 1-7
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1-7
    • Thweatt, R.1    Lumpkin, C.K.2    Goldstein, S.3
  • 40
    • 1642418213 scopus 로고    scopus 로고
    • Ablation of SM22alpha decreases contractility and actin contents of mouse vascular smooth muscle
    • Zeidan A., Sward K., Nordstrom I., Ekblad E., Zhang J.C., Parmacek M.S., and Hellstrand P. Ablation of SM22alpha decreases contractility and actin contents of mouse vascular smooth muscle. FEBS Lett. 562 (2004) 141-146
    • (2004) FEBS Lett. , vol.562 , pp. 141-146
    • Zeidan, A.1    Sward, K.2    Nordstrom, I.3    Ekblad, E.4    Zhang, J.C.5    Parmacek, M.S.6    Hellstrand, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.