The three-dimensional structure of a type I module from titin: A prototype of intracellular fibronectin type III domains

Structure

Volumn 6, Issue 10, 1998, Pages 1291-1302

  Muhle Goll, C ^a,b   Pastore, A ^a,c   Nilges, M ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

Connectin; Fibronectin type III; Modelling; Muscle; NMR

Indexed keywords

ANIMALIA;

EID: 0038083197     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0969-2126(98)00129-4     Document Type: Article

References (51)

1. Maruyama, K., et al., & Eguchi, G. (1977). Connectin, an elastic protein of muscle: characterization and function. J. Biochem. (Tokyo) 82, 317-337.
2. Wang, K., McClure, J. & Tu, A. (1979). Titin: major myofibrillar components of striated muscle. Proc. Natl Acad. Sci. USA 76, 3698-3702.
3. Magid, A. & Law, D.J. (1985). Myofibrils bear most of the resting tension in frog skeletal muscle. Science 230, 1280-1282.
4. Huxley, A.F. & Niedergerke, (1954). Structural changes in muscle during contraction. Nature 173, 971-972.
5. Huxley, H.E. & Hanson, J. (1954). Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 173, 973-976.
6. Nave, R., Fürst, D.O. & Weber, K. (1989). Visualization of the polarity isolated titin molecules: a single globular head on a long thin rod as the m-band anchoring domain? J. Cell Biol. 109, 2177-2187.
7. Labeit, S. & Kolmerer, B. (1995). Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270, 293-296.
8. Benian, G.M., Kiff, J.E., Neckelmann, N., Moerman, D.G. & Waterston, R.H. (1989). Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans. Nature 342, 45-50.
9. Labeit, S., et al., & Trinick, J. (1990). A regular pattern of two types of 100-residue motif in the sequence of titin. Nature 345, 273-276.
10. Craig, R. (1977). Stucture of a-segments from frog and rabbit skeletal muscle. J. Mol. Biol. 109, 69-81.
11. Sjöström, M. & Squire, J. (1977). Fine structure of the A-band in cryo-sections: the structure of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J. Mol. Biol. 109, 49-68.
12. Fürst, D.O., Vinkemeyer, U. & Weber, K. (1992). Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full-length cDNA. J. Cell Sci. 102, 769-778.
13. Labeit, S., Gautel, M., Lakey, A. & Trinick, J. (1992). Towards a molecular understanding of titin. EMBO J. 11, 1711-1716.
14. Soteriou, A., Gamage, M. & Trinick, J. (1993). A survey of interactions made by the giant muscle protein titin. J. Cell Sci. 104, 119-123.
15. Houmeida, A., Holt, J., Tskhovrebova, L. & Trinick, J. (1995). Studies of the interaction between titin and myosin. J. Cell Biol. 131, 1471-1481.
16. Freiburg, A. & Gautel, M. (1996). A molecular map of the interactions between titin and myosin-binding protein c. implications for sarcomeric assembly in familial hypertrophie cardiomyopathy. Eur. J. Biochem. 235, 317-323.
17. Politou, A.S., Gautel, M., Lambeit, S. & Pastore, A. (1994). Immunoglobulin-type domains of titin: same fold, different stability? Biochemistry 4730-4737.
18. Politou, A.S., Gautel, M., Improta, S., Vangelista, L & Pastore, A. (1996). The elastic I-band region of titin is assembled in a modular fashion by weakly interacting Ig-like domains., J. Mol. Biol. 255, 604-616.
19. Pfuhl, M. & Pastore, A. (1995). Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the I set. Structures 3, 391-401.
20. Improta, S., Politou, A.S. & Pastore, A. (1996). Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. Structure 4, 323-337.
21. 15N NMR resonance assignments and secondary structure of titin type I domains. J. Biomol. NMR 9, 2-10.
22. Nilges, M., Macias, M.J., O'Donoghue, S. & Oschkinat, H. (1997). Automated NOESY interpretation with ambiguous distance restraints: the refined solution structure of the pleckstrin homology domain from β-spectrin. J. Mol. Biol. 269, 408-422.
23. Brünger, A.T. (1992). X-PLOR. A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
24. Nilges, M. (1995). Calculation of protein structures with ambiguous distance restraints, automated assignment of ambiguous NOE crosspeaks and disulphide connectivities. J. Mol. Biol. 245, 645-660.
25. Huber, A.W., Wang, Y.E., Bieber, A.J. & Bjorkman, P.J. (1994). Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A. Neuron 12, 717-731.
26. Antz, C., Neidig, K.P. & Kalbitzer, H.R. (1995). A general Bayesian method for an automated signal class recognition in 2D NMR spectra combined with a multivariate discriminant analysis. J. Biomol. NMR 5, 287-296.
27. Sunnerhagen, M., Nilges, M., Otting, G. & Carey, J. (1997). Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA. Nat. Struct. Biol. 4, 819-826.
28. Wilmot, C.M. & Thornton, J.M. (1990). β Turns and their distortions: a proposed new nomenclature. Protein Eng. 9, 479-493.
29. Chan, A.W., Hutchinson, E.G., Harris, D. & Thornton, J.M. (1993). Identification, classification and analysis of β-bulges in proteins. Protein Sci. 2, 1574-1590.
30. Mitchell, J.B.O., Nandi, C.L.I.K., McDonald, I.K. & Thornton, J.M. (1994). Amino/aromatic interactions in proteins: is the evidence stacked against hydrogen bonding? J. Mol. Biol. 239, 315-331.
31. Spitzfaden, C., Grant, R.P., Mardon, H.J. & Campbell, I.D. (1997). Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. J. Mol. Biol. 265, 565-579.
32. Leahy, D.J., Aukhil, I. & Erickson, H.P. (1996). 2.0 Å Crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155-164.
33. Muller, Y.A., Ultsch, M.H. & de Vos, A.M. (1996). The crystal structure of the extracellular domain of human tissue factor refined to 1.7 A resolution. J. Mol. Biol. 256, 144-159.
34. Higgins, D.G., Labeit, S., Gautel, M. & Gibson, T.J. (1994). The evolution of titin and related giant muscle proteins., J. Mol. Evol. 38, 395-404.
35. Improta, S., et al, & Pastore, A. (1998). The assembly of immunoglobulin-like modules in titin: implications for muscle elasticity. J. Mol. Biol., in press.
36. Main, A.L., Harvey, T.S., Baron, M., Boyd, J. & Campbell, I.D. (1992). The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71, 671-678.
37. Leahy, D.J., Hendrickson, W., Aukhil, I. & Erickson, H.P. (1992). Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258, 987-991.
38. de Vos, A.M., Ultsch, M. & Kossiakoff, A.A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312.
39. Williamson, M.P. (1994). The structure and function of proline-rich regions in proteins. Biochem. J. 297, 249-260.
40. Craig, R. & Offer, G. (1976). The location of c-protein in rabbit skeletal muscle. Proc. R. Soc. Lond. B 192, 451-461.
41. Bennett, P.M. & Gautel, M. (1996). Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament. J. Mol. Biol. 259, 896-903.
42. Neidig, P., et al., & Kalbitzer, H.R. (1995). AURELIA, a program for computer-aided analysis of multidimensional NMR spectra. J. Biomol. NMR 6, 255-270.
43. 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 31, 5269-5278.
44. Nilges, M. & O'Donoghue, S.I. (1998). Ambiguous NOEs and automated NOESY assignment. J. Mol. Biol. 269, 408-422.
45. Folmer, R.H.A., Konings, R.N.H., Hilbers, C.W. & Nilges, M. (1997). Stereospecific assignment revisited: application to an 18 kDa protein and comparison with j coupling data. J. Biomol. NMR 9, 245-258.
46. Rice, L.M. & Brünger, AT. (1994). Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19, 277-290.
47. Stein, E.G., Rice, L.M. & Brünger, AT. (1997). Torsion angle molecular dynamics as a new efficient tool for NMR structure calculation. J. Magn. Reson. 124, 154-164.
48. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
49. Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. & Higgins, D.G. (1997). The CLUSTALX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
50. Vriend, G. (1990). What if: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-55.
51. Sippl, M.J. (1993). Recognition of errors in three-dimensional structures of proteins. Proteins 17, 355-362.