[HTML][HTML] Structure and dynamics of the human muscle LIM protein
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 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 …
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.
Elsevier