Key result
NMR spectroscopy confirms human MLP LIM domains act as independent units with fully flexible linkers.
The structural characterization of human muscle LIM protein completes the structural determination of the cysteine rich protein (CRP) family.
Does not alter clinical practice; completes CRP family structural database for future mechanistic studies.
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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Schallus et al. (2009) studied this question. Nuclear magnetic resonance spectroscopy determined the structure of both LIM domains of human MLP, confirming they act as independent units with fully flexible adjacent linker regions.
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