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Structure and dynamics of the human muscle LIM protein
Author(s) -
Schallus Thomas,
Fehér Krisztina,
Ulrich Anne S.,
Stier Gunter,
Muhle-Goll Claudia
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.02.021
Subject(s) - myogenesis , lim domain , myofibril , chemistry , linker , microbiology and biotechnology , skeletal muscle , regulator , biophysics , biology , anatomy , biochemistry , gene , zinc finger , computer science , transcription factor , operating system
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 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.