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Volumn 290, Issue 2, 1999, Pages 581-593

Modularity and homology: Modelling of the type II module family from titin

Author keywords

Connectin; Dynamics; I set; Immunoglobulin; Muscle

Indexed keywords

CONNECTIN;

EID: 0033538417     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2876     Document Type: Article
Times cited : (28)

References (69)
  • 1
    • 0029866846 scopus 로고    scopus 로고
    • Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water
    • Berndt K. D., Güntert P., Wüthrich K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water. Proteins: Struct. Funct. Genet. 24:1996;304-313.
    • (1996) Proteins: Struct. Funct. Genet. , vol.24 , pp. 304-313
    • Berndt, K.D.1    Güntert, P.2    Wüthrich, K.3
  • 2
    • 0028172534 scopus 로고
    • The immunoglobulin fold: Structural classification, sequence patterns and common core
    • Bork P., Holm L., Sander C. The immunoglobulin fold: structural classification, sequence patterns and common core. J. Mol. Biol. 242:1994;309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 5
    • 0027304152 scopus 로고
    • Hydration of proteins: A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations
    • Brunne R. M., Liepinsh E., Otting O., Wüthrich K., van Gunsteren W. F. Hydration of proteins: a comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations. J. Mol. Biol. 231:1993;1040-1048.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1040-1048
    • Brunne, R.M.1    Liepinsh, E.2    Otting, O.3    Wüthrich, K.4    Van Gunsteren, W.F.5
  • 6
    • 0020483945 scopus 로고
    • Evolution of proteins formed by beta-sheets. I. plastocyanin and azurin
    • Chothia C., Lesk A. M. Evolution of proteins formed by beta-sheets. I. plastocyanin and azurin. J. Mol. Biol. 160:1982a;309-323.
    • (1982) J. Mol. Biol. , vol.160 , pp. 309-323
    • Chothia, C.1    Lesk, A.M.2
  • 7
    • 0020429363 scopus 로고
    • Evolution of proteins formed by beta-sheets. II. The core of the immunoglobulin domains
    • Chothia C., Lesk A. M. Evolution of proteins formed by beta-sheets. II. The core of the immunoglobulin domains. J. Mol. Biol. 160:1982b;325-342.
    • (1982) J. Mol. Biol. , vol.160 , pp. 325-342
    • Chothia, C.1    Lesk, A.M.2
  • 8
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C., Lesk A. M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:1986;823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 10
    • 0019858614 scopus 로고
    • Similar amino-acid sequences: Change or common ancestry
    • Doolittle R. F. Similar amino-acid sequences: change or common ancestry. Science. 214:1981;149-159.
    • (1981) Science , vol.214 , pp. 149-159
    • Doolittle, R.F.1
  • 11
    • 0027364941 scopus 로고
    • Evolutionarily mobile modules in proteins
    • Doolittle R. F., Bork P. Evolutionarily mobile modules in proteins. Sci. Am. 269:1993;50-56.
    • (1993) Sci. Am. , vol.269 , pp. 50-56
    • Doolittle, R.F.1    Bork, P.2
  • 12
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg A., Gautel M. A molecular map of interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 235:1996;317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 13
    • 0027448024 scopus 로고
    • Elastic filaments in situ in cardiac muscles: Deep-etch replica analysis in combination with selective removal of actin and myosin filaments
    • Funatsu T., Kono E., Higuchi H., Kimura S., Ishiwata S., Yoshioka T., Maruyama K., Tsukika S. Elastic filaments in situ in cardiac muscles: deep-etch replica analysis in combination with selective removal of actin and myosin filaments. J. Cell Biol. 120:1993;711-724.
    • (1993) J. Cell Biol. , vol.120 , pp. 711-724
    • Funatsu, T.1    Kono, E.2    Higuchi, H.3    Kimura, S.4    Ishiwata, S.5    Yoshioka, T.6    Maruyama, K.7    Tsukika, S.8
  • 14
    • 0029824116 scopus 로고    scopus 로고
    • The super-repeats of titin/connectin and their interactions: Glimpses at sarcomeric assembly
    • Gautel M. The super-repeats of titin/connectin and their interactions: glimpses at sarcomeric assembly. Advan. Biophys. 33:1996;27-37.
    • (1996) Advan. Biophys. , vol.33 , pp. 27-37
    • Gautel, M.1
  • 15
    • 0029859276 scopus 로고    scopus 로고
    • The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers
    • Gautel M., Goulding D., Bullard B., Weber K., Fürst D. O. The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers. J. Cell Sci. 109:1996;2747-2754.
    • (1996) J. Cell Sci. , vol.109 , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Fürst, D.O.5
  • 18
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz Y., Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238:1994;528-532.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-532
    • Harpaz, Y.1    Chothia, C.2
  • 19
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 20
    • 0024426462 scopus 로고
    • Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle
    • Horowits R., Maruyama K., Podolsky R. J. Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle. J. Cell Biol. 109:1989;2169-2176.
    • (1989) J. Cell Biol. , vol.109 , pp. 2169-2176
    • Horowits, R.1    Maruyama, K.2    Podolsky, R.J.3
  • 21
    • 0033577911 scopus 로고    scopus 로고
    • Molecular evolution of immunoglobulin and fibronectin domains in titin and related muscle proteins
    • Kenny P. A., Liston E. M., Higgins D. G. Molecular evolution of immunoglobulin and fibronectin domains in titin and related muscle proteins. Gene. 232:1999;11-23.
    • (1999) Gene , vol.232 , pp. 11-23
    • Kenny, P.A.1    Liston, E.M.2    Higgins, D.G.3
  • 22
    • 0031241809 scopus 로고    scopus 로고
    • Protein solution structure calculations in solution: Solvated molecular dynamics refinement of calbidin D9k
    • Koerdel J., Pearlman D. A., Chazin W. J. Protein solution structure calculations in solution: solvated molecular dynamics refinement of calbidin D9k. J. Biomol. NMR. 10:1997;231-243.
    • (1997) J. Biomol. NMR , vol.10 , pp. 231-243
    • Koerdel, J.1    Pearlman, D.A.2    Chazin, W.J.3
  • 23
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • Improta S., Politou A. S., Pastore A. Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. Structure. 4:1996;323-337.
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 25
    • 0028824480 scopus 로고
    • Titins, giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S., Kolmerer B. Titins, giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:1995;293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 27
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., McArthur M. W., Moss D. S., Thornton J. M. 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.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0030997363 scopus 로고    scopus 로고
    • Hydrophobic patches on protein subunit interfaces: Characteristics and prediction
    • Lijnzaad P., Argos P. Hydrophobic patches on protein subunit interfaces: characteristics and prediction. Proteins: Struct. Funct. Genet. 28:1997;333-343.
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 333-343
    • Lijnzaad, P.1    Argos, P.2
  • 31
  • 32
    • 0031809493 scopus 로고    scopus 로고
    • Characterizing titin's I-band Ig domain region as an entropic spring
    • Linke W. A., Stockmeier M. R., Ivemeyer M., Hosser H., Mundel P. Characterizing titin's I-band Ig domain region as an entropic spring. J. Cell Sci. 111:1998;1567-1574.
    • (1998) J. Cell Sci. , vol.111 , pp. 1567-1574
    • Linke, W.A.1    Stockmeier, M.R.2    Ivemeyer, M.3    Hosser, H.4    Mundel, P.5
  • 35
    • 0030982846 scopus 로고    scopus 로고
    • Connecting/titin, giant elastic protein of muscle
    • Maruyama K. Connecting/titin, giant elastic protein of muscle. FASEB J. 11:1997;341-345.
    • (1997) FASEB J. , vol.11 , pp. 341-345
    • Maruyama, K.1
  • 36
    • 0023645203 scopus 로고
    • The interior and surface of monomeric proteins
    • Miller S., Janin J., Lesk A. M., Chothia C. The interior and surface of monomeric proteins. J. Mol. Biol. 196:1987;641-657.
    • (1987) J. Mol. Biol. , vol.196 , pp. 641-657
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4
  • 37
    • 0028864205 scopus 로고
    • A critical assessment of comparative molecular modeling of tertiary structures of proteins
    • Mosimann S., Meleshko R., James M. N. G. A critical assessment of comparative molecular modeling of tertiary structures of proteins. Proteins: Struct. Funct. Genet. 23:1995;301-317.
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 301-317
    • Mosimann, S.1    Meleshko, R.2    James, M.N.G.3
  • 39
    • 0032557642 scopus 로고    scopus 로고
    • Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin
    • Mues A., van der Ven P. F., Young P., Furst D. O., Gautel M. Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin. FEBS Letters. 428:1998;111-114.
    • (1998) FEBS Letters , vol.428 , pp. 111-114
    • Mues, A.1    Van Der Ven, P.F.2    Young, P.3    Furst, D.O.4    Gautel, M.5
  • 40
    • 0038083197 scopus 로고    scopus 로고
    • The 3D structure of a type I module from titin: A prototype of intracellular fibronectin type III domains
    • Muhle Goll C., Pastore A., Nilges M. The 3D structure of a type I module from titin: a prototype of intracellular fibronectin type III domains. Structure. 6:1998;1291-1302.
    • (1998) Structure , vol.6 , pp. 1291-1302
    • Muhle Goll, C.1    Pastore, A.2    Nilges, M.3
  • 41
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
    • Obermann W. M. J., Gautel M., Weber K., Fuerst D. O. Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO J. 16:1997;211-220.
    • (1997) EMBO J. , vol.16 , pp. 211-220
    • Obermann, W.M.J.1    Gautel, M.2    Weber, K.3    Fuerst, D.O.4
  • 42
    • 0031027371 scopus 로고    scopus 로고
    • Binding of the N-terminal fragment of connectin/titin to α-actinin as revealed by yeast two-hybrid system
    • Ohtsuka H., Yajima H., Kimura S., Maruyama K. Binding of the N-terminal fragment of connectin/titin to α-actinin as revealed by yeast two-hybrid system. FEBS Letters. 401:1997;65-67.
    • (1997) FEBS Letters , vol.401 , pp. 65-67
    • Ohtsuka, H.1    Yajima, H.2    Kimura, S.3    Maruyama, K.4
  • 43
    • 0026211201 scopus 로고
    • Brave new proteins: What evolution reveals about protein structure
    • Pastore A., Lesk A. Brave new proteins: what evolution reveals about protein structure. Curr. Opin. Biotechnol. 2:1991;592-598.
    • (1991) Curr. Opin. Biotechnol. , vol.2 , pp. 592-598
    • Pastore, A.1    Lesk, A.2
  • 44
    • 0029644479 scopus 로고
    • Tertiary structure of an Ig-like domain from a giant muscle protein titin: A new member of the I set
    • Pfuhl M., Pastore A. Tertiary structure of an Ig-like domain from a giant muscle protein titin: a new member of the I set. Structure. 3:1995;391-401.
    • (1995) Structure , vol.3 , pp. 391-401
    • Pfuhl, M.1    Pastore, A.2
  • 45
    • 0031575331 scopus 로고    scopus 로고
    • When a module is also a domain: The role of the N terminus in the stability and the dynamics of immunoglobulin domains from titin
    • Pfuhl M., Improta S., Politous A. S., Pastore A. When a module is also a domain: the role of the N terminus in the stability and the dynamics of immunoglobulin domains from titin. J. Mol. Biol. 265:1997;242-256.
    • (1997) J. Mol. Biol. , vol.265 , pp. 242-256
    • Pfuhl, M.1    Improta, S.2    Politous, A.S.3    Pastore, A.4
  • 46
    • 0029361476 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A. Comparative protein modeling by satisfaction of spatial restraints. Mol. Med. Today. 1:1995;270-277.
    • (1995) Mol. Med. Today , vol.1 , pp. 270-277
    • Sali, A.1
  • 47
    • 0031787022 scopus 로고    scopus 로고
    • 100,000 protein structures for the biologist
    • Sali A. 100,000 protein structures for the biologist. Nature Struct. Biol. 5:1998;1029-1032.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1029-1032
    • Sali, A.1
  • 48
    • 0027136282 scopus 로고
    • Comparative modelling by satisfaction of spatial restraints
    • Sali A., Blundell T. L. Comparative modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 49
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • Sali A., Overington J. P. Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci. 3:1994;1582-1596.
    • (1994) Protein Sci. , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 51
    • 0031307019 scopus 로고    scopus 로고
    • Evaluation of comparative protein structure modeling by MODELLER-3
    • Sanchez R., Sali A. Evaluation of comparative protein structure modeling by MODELLER-3. Proteins: Struct. Funct. Genet. Suppl. 1:1997;50-58.
    • (1997) Proteins: Struct. Funct. Genet. , vol.1 , pp. 50-58
    • Sanchez, R.1    Sali, A.2
  • 52
    • 0032506030 scopus 로고    scopus 로고
    • Large-scale protein structure modeling of the saccharomyces cerevisiae genome
    • Sanchez R., Sali A. Large-scale protein structure modeling of the saccharomyces cerevisiae genome. Proc. Natl Acad. Sci. USA. 95:1998;13597-13602.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13597-13602
    • Sanchez, R.1    Sali, A.2
  • 53
    • 0026030641 scopus 로고
    • Database of homology derived protein structures and the structural meaning of sequence alignment
    • Sander C., Schneider R. Database of homology derived protein structures and the structural meaning of sequence alignment. Proteins: Struct. Funct. Genet. 9:1991;56-68.
    • (1991) Proteins: Struct. Funct. Genet. , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 54
    • 0032581907 scopus 로고    scopus 로고
    • Practical evaluation of comparative modelling and threading methods
    • Schoonman M. J., Knegtel R. M., Grootenhuis P. D. Practical evaluation of comparative modelling and threading methods. Comput. Chem. 22:1998;369-375.
    • (1998) Comput. Chem. , vol.22 , pp. 369-375
    • Schoonman, M.J.1    Knegtel, R.M.2    Grootenhuis, P.D.3
  • 55
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl M. J. Recognition of errors in three-dimensional structures of proteins. Proteins: Struct. Funct. Genet. 17:1993;355-362.
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 57
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTALX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J. D., Gibson T. J., Plewniak F., Jeanmougin F., Higgins D. G. The CLUSTALX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 25:1997;4876-4882.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 58
    • 0031717909 scopus 로고    scopus 로고
    • Homology modeling with low sequence identity
    • Tramontano A. Homology modeling with low sequence identity. Methods. 14:1998;293-300.
    • (1998) Methods , vol.14 , pp. 293-300
    • Tramontano, A.1
  • 59
    • 0030091595 scopus 로고    scopus 로고
    • Cytoskeleton: Titin as a scaffold and spring
    • Trinick J. Cytoskeleton: titin as a scaffold and spring. Curr. Biol. 6:1996;258-260.
    • (1996) Curr. Biol. , vol.6 , pp. 258-260
    • Trinick, J.1
  • 60
    • 0027313537 scopus 로고
    • Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle
    • Trombitas K., Pollack G. H. Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle. J. Muscle Res. Cell Motil. 14:1993;416-422.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 416-422
    • Trombitas, K.1    Pollack, G.H.2
  • 61
    • 0031691961 scopus 로고    scopus 로고
    • PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10
    • Trombitas K., Greaser M., French G., Granzier H. PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10. J. Struct. Biol. 122:1998;188-196.
    • (1998) J. Struct. Biol. , vol.122 , pp. 188-196
    • Trombitas, K.1    Greaser, M.2    French, G.3    Granzier, H.4
  • 64
  • 65
    • 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;52-55.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-55
    • Vriend, G.1
  • 66
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of alpha-actin
    • Young P., Ferguson C., Banuelos S., Gautel M. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actin. EMBO J. 17:1998;1614-1624.
    • (1998) EMBO J. , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4
  • 67
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension
    • Wang K., McCarter R., Wright J., Beverly J., Ramirez-Mitchell R. Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension. Proc. Natl Acad. Sci. USA. 88:1991;7101-7105.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Wright, J.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 68
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting A. J., Wardale J., Trinick J. Does titin regulate the length of muscle thick filaments? J. Mol. Biol. 205:1989;163-169.
    • (1989) J. Mol. Biol. , vol.205 , pp. 163-169
    • Whiting, A.J.1    Wardale, J.2    Trinick, J.3


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