The Ig Doublet Z1Z2: A Model System for the Hybrid Analysis of Conformational Dynamics in Ig Tandems from Titin

Structure

Volumn 14, Issue 9, 2006, Pages 1437-1447

  Marino, Marco ^a   Zou, Peijian ^b   Svergun, Dmitri ^b,c   Garcia, Pilar ^a   Edlich, Christian ^d   Simon, Bernd ^d   Wilmanns, Matthias ^b   Muhle Goll, Claudia ^d,e   Mayans, Olga ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b DESY   (Germany)

^c SHUBNIKOV INSTITUTE OF CRYSTALLOGRAPHY   (Russian Federation)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^e MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; IMMUNOGLOBULIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATION; CRYSTAL STRUCTURE; DYNAMICS; HUMAN; HYBRID; HYDROPHOBICITY; MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SARCOMERE; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; HUMANS; IMMUNOGLOBULINS; MODELS, MOLECULAR; MUSCLE PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN KINASES; SPECTRUM ANALYSIS;

VERTEBRATA;

EID: 33748331350     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.07.009     Document Type: Article

References (44)

1. Bax A., Kontaxis G., and Tjandra N. Dipolar couplings in macromolecular structure determination. Methods Enzymol. 339 (2001) 127-174
2. Bertini I., Del Bianco C., Gelis I., Katsaros N., Luchinat C., Parigi G., Peana M., Provenzani A., and Zoroddu M.A. Experimentally exploring the conformational space sampled by domain reorientation in calmodulin. Proc. Natl. Acad. Sci. USA 101 (2004) 6841-6846
3. Boggon T.J., Murray J., Chappuis-Flament S., Wong E., Gumbiner B.M., and Shapiro L.C. Cadherin ectodomain structure and implications for cell adhesion mechanisms. Science 296 (2002) 1308-1313
4. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
5. CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
6. Cierpicki T., and Bushweller J.H. Charged gels as orienting media for measurement of residual dipolar couplings in soluble and integral membrane proteins. J. Am. Chem. Soc. 126 (2004) 16259-16266
7. Clore G.M., Gronenborn A.M., and Tjandra N. Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude. J. Magn. Reson. 131 (1998) 159-162
8. Cornilescu G., Marquardt J.L., Ottiger M., and Bax A. Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J. Am. Chem. Soc. 120 (1998) 6836-6837
9. Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
10. Dosset P., Hus J.C., Blackledge M., and Marion D. Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J. Biomol. NMR 16 (2000) 23-28
11. Edlich C., and Muhle-Goll C. 1H, 13C, and 15N backbone assignment of the first two Ig domains Z1Z2 of the giant muscle protein Titin. J. Biomol. NMR 27 (2003) 283-284
12. Evans, P.R. (1993). Data reduction. Proceedings of CCP4 Study Weekend on Data Collection and Processing, 114-122.
13. Feigin L.A., and Svergun D.I. Structure Analysis by Small-Angle X-Ray and Neutron Scattering (1987), Plenum Press, New York
14. Freigang J., Proba K., Leder L., Diederichs K., Sonderegger P., and Welte W. The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion. Cell 101 (2000) 425-433
15. Granzier H.L., and Labeit S. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ. Res. 94 (2004) 284-295
16. Gregorio C.C., Trombitas K., Centner T., Kolmerer B., Stier G., Kunke K., Suzuki K., Obermayr F., Herrmann B., Granzier H., et al. The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J. Cell Biol. 143 (1998) 1013-1027
17. Harpaz Y., and 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) 528-539
18. Häussinger D., Ahrens T., Sass H.J., Pertz O., Engel J., and Grzesiek S. Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions. J. Mol. Biol. 324 (2002) 823-839
19. Hayward S., and Lee R.A. Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50. J. Mol. Graph. Model. 21 (2002) 181-183
20. Improta S., Krueger J.K., Gautel M., Atkinson R.A., Lefevre J.F., Moulton S., Trewhella J., and Pastore A. The assembly of immunoglobulin-like modules in titin: implications for muscle elasticity. J. Mol. Biol. 284 (1998) 761-777
21. 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
22. Konarev P.V., Volkov V.V., Sokolova A.V., Koch M.H.J., and Svergun D.I. PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J. Appl. Crystallogr. 36 (2003) 1277-1282
23. Leahy D.J., Aukhil I., and Erickson H.P. 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84 (1996) 155-164
24. Leslie, A.G.W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography.
25. Linge J.P., O'Donoghue S.I., and Nilges M. Automated assignment of ambiguous nuclear overhauser effects with ARIA. Methods Enzymol. 339 (2001) 71-90
26. Losonczi J.A., Andrec M., Fischer M.W., and Prestegard J.H. Order matrix analysis of residual dipolar couplings using singular value decomposition. J. Magn. Reson. 138 (1999) 334-342
27. Lu G. TOP: a new method for protein structure comparisons and similarity searches. J. Appl. Crystallogr. 33 (2000) 176-183
28. Luzatti V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallogr. 5 (1952) 802-810
29. Marino M., Svergun D.I., Kreplak L., Konarev P.V., Maco B., Labeit D., and Mayans O. Poly-Ig tandems from I-band titin share extended domain arrangements irrespective of the distinct features of their modular constituents. J. Muscle Res. Cell Motil. 36 (2005) 355-365
30. Mues A., van der Ven P.F., Young P., Furst D.O., and Gautel M. Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation dependent way with telethonin. FEBS Lett. 428 (1998) 111-114
31. Navaza J. Implementation of molecular replacement in AMoRe. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1367-1372
32. Perrakis A., Harkiolaki M., Wilson K.S., and Lamzin V.S. ARP/wARP and molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1445-1450
33. Politou A.S., Gautel M., Improta S., Vangelista L., and Pastore A. The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains. J. Mol. Biol. 255 (1996) 604-616
34. Scott K.A., Steward A., Fowler S.B., and Clarke J. Titin; a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315 (2002) 819-829
35. Soroka V., Kolkova K., Kastrup J.S., Diederichs K., Breed J., Kiselyov V.V., Poulsen F.M., Larsen I.K., Welte W., Berezin V., et al. Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion. Structure 11 (2003) 1291-1301
36. Spitzfaden C., Grant R.P., Mardon H.J., and Campbell I.D. Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. J. Mol. Biol. 265 (1997) 565-579
37. Su X.D., Gastinel L.N., Vaughn D.E., Faye I., Poon P., and Bjorkman P.J. Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion. Science 281 (1998) 991-995
38. Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL-a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
39. Svergun D.I., Petoukhov M.V., and Koch M.H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
40. Tjandra N., Omichinski J.G., Gronenborn A.M., Clore G.M., and Bax A. Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nat. Struct. Biol. 4 (1997) 732-738
41. Ulmer T.S., Ramirez B.E., Delaglio F., and Bax A. Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. J. Am. Chem. Soc. 125 (2003) 9179-9191
42. Zou P., Gautel M., Geerlof A., Wilmanns M., Koch M.H., and Svergun D.I. Solution scattering suggests cross-linking function of telethonin in the complex with titin. J. Biol. Chem. 278 (2003) 2636-2644
43. Zou P., Pinotsis N., Lange S., Song Y.H., Popov A., Mavridis I., Mayans O., Gautel M., and Wilmanns M. Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk. Nature 439 (2006) 229-233
44. Zweckstetter M., and Bax A. Evaluation of uncertainty in alignment tensors obtained from dipolar couplings. J. Biomol. NMR 23 (2002) 127-137