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  Structure and dynamics of the human muscle LIM protein

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.

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FEBSLett_583_2009_1017.pdf (Any fulltext), 2MB
 
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Schallus, Thomas1, Author           
Fehér, Krisztina1, Author           
Ulrich, Anne S., Author
Stier, Gunter1, Author           
Muhle-Goll, Claudia1, Author           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Cysteine rich protein; NMR; α-Actinin; Telethonin
 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.

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Language(s): eng - English
 Dates: 2009-02-102008-12-222009-02-112009-02-212009-03-18
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 583 (6) Sequence Number: - Start / End Page: 1017 - 1022 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501