Structure and dynamics of the human muscle LIM protein

Schallus, Thomas; Fehér, Krisztina; Ulrich, Anne S.; Stier, Gunter; Muhle-Goll, Claudia

doi:10.1016/j.febslet.2009.02.021

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Volume 583, Issue 6 , Pages 1017-1022, 18 March 2009

Structure and dynamics of the human muscle LIM protein

Edited by Hans Eklund

Thomas Schallus
- Department of Biomolecular Mechanisms, Max-Planck-Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany
- Department of Structures and Biocomputing, EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany
Krisztina Fehér
- Department of Biomolecular Mechanisms, Max-Planck-Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany
- Department of Structures and Biocomputing, EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany
Anne S. Ulrich
- Karlsruhe Institute of Technology (KIT), Institut für Biologische Grenzflächen (IBG-2), P.O. Box 3640, 76021 Karlsruhe, Germany
Gunter Stier
- Department of Biomolecular Mechanisms, Max-Planck-Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany
- Present address: Department of Biomolecular Mechanisms, Max-Planck-Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.
Claudia Muhle-Goll
- Karlsruhe Institute of Technology (KIT), Institut für Biologische Grenzflächen (IBG-2), P.O. Box 3640, 76021 Karlsruhe, Germany
- Corresponding author. Fax: +49 721 608 4823.

Received 22 December 2008; received in revised form 10 February 2009; accepted 11 February 2009. published online 20 February 2009.

Abstract

The family of cysteine rich proteins (CRP) comprises three closely homologous members that have been reported to interact with α-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 ¹⁵N 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.

Abbreviations: CRP, cysteine rich protein, HSQC, heteronuclear single quantum coherence, LIM1, N-terminal LIM domain of MLP, LIM2, C-terminal LIM domain of MLP, MLP, muscular LIM protein, NOE, nuclear overhauser effect, NOESY, nuclear overhauser enhancement spectroscopy, hetNOE, heteronuclear NOE, RMSD, root mean square deviation.