The Ig doublet Z1Z2 : a model system for the hybrid analysis of conformational dynamics in Ig tandems from titin

Marino, M. and Zou, P. and Svergun, D. and Garcia, P. and Edlich, C. and Simon, B. and Wilmanns, M. and Muhle-Goll, C. and Mayans, O.. (2006) The Ig doublet Z1Z2 : a model system for the hybrid analysis of conformational dynamics in Ig tandems from titin. Structure: with folding and design, Vol. 14, H. 9. pp. 1437-1447.

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Official URL: http://edoc.unibas.ch/dok/A5259367

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Titin is a gigantic elastic filament that determines sarcomere ultrastructure and stretch response in vertebrate muscle. It folds into numerous Ig and FnIII domains connected in tandem. Data on interdomain arrangements and dynamics are essential for understanding the function of this filament. Here, we report a mechanistic analysis of the conformational dynamics of two Ig domains from the N terminus of titin, Z1Z2, by using X-ray crystallography, SAXS, NMR relaxation data, and residual dipolar couplings in combination. Z1Z2 preferentially adopts semiextended conformations in solution, with close-hinge arrangements representing low-probability states. Although interdomain contacts are not observed, the linker appears to acquire moderate rigidity via small, local hydrophobic interactions. Thus, Z1Z2 constitutes an adaptable modular system with restricted dynamics. We speculate that its preexistent conformation contributes to the selective recruitment of the binding partner telethonin onto the repetitive surface of the filament. The structural interconversion of four Z1Z2 conformers is analyzed.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Mayans)
UniBasel Contributors:Mayans, Olga
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Current Biology
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:22
Deposited On:22 Mar 2012 13:31

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