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Journal Article

Structure and dynamics of the human muscle LIM protein

MPS-Authors
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Schallus,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Fehér,  Krisztina
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117899

Stier,  Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94456

Muhle-Goll,  Claudia
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2009.02.021/epdf
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https://dx.doi.org/10.1016/j.febslet.2009.02.021
(Any fulltext)

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Citation

Schallus, T., Fehér, K., Ulrich, A. S., Stier, G., & Muhle-Goll, C. (2009). Structure and dynamics of the human muscle LIM protein. FEBS Letters, 583(6), 1017-1022. doi:10.1016/j.febslet.2009.02.021.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-15DB-2
Abstract
The family of cysteine rich proteins (CRP) comprises three closely homologous members that have been reported to interact with alpha-actinin. Muscular LIM protein (MLP/CRP3), the skeletal muscle variant, was originally discovered as a positive regulator of myogenesis and is suggested to be part of the stretch sensor of the myofibril through its interaction with telethonin (T-Cap). We determined the structure of both LIM domains of human MLP by nuclear magnetic resonance spectroscopy. We confirm by (15)N relaxation measurements that both LIM domains act as independent units and that the adjacent linker regions are fully flexible. With the published structures of CRP1 and CRP2, the complete family has now been structurally characterized.