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 s...

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Veröffentlicht in:FEBS letters 2009-03, Vol.583 (6), p.1017-1022
Hauptverfasser: Schallus, Thomas, Fehér, Krisztina, Ulrich, Anne S., Stier, Gunter, Muhle-Goll, Claudia
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container_end_page 1022
container_issue 6
container_start_page 1017
container_title FEBS letters
container_volume 583
creator Schallus, Thomas
Fehér, Krisztina
Ulrich, Anne S.
Stier, Gunter
Muhle-Goll, Claudia
description 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.
doi_str_mv 10.1016/j.febslet.2009.02.021
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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. 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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. 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subjects Adaptor Proteins, Signal Transducing
Animals
Avian Proteins - chemistry
C-terminal LIM domain of MLP
Carrier Proteins - chemistry
CRP
Cysteine rich protein
DNA-Binding Proteins - chemistry
Eye Proteins - chemistry
heteronuclear NOE
heteronuclear single quantum coherence
hetNOE
Homeodomain Proteins - chemistry
HSQC
Humans
LIM Domain Proteins
LIM-Homeodomain Proteins
LIM1
LIM2
Membrane Proteins
MLP
Models, Molecular
Muscle Proteins - chemistry
Muscle Proteins - genetics
Muscle Proteins - physiology
muscular LIM protein
N-terminal LIM domain of MLP
NMR
NOE
NOESY
Nuclear Magnetic Resonance, Biomolecular
nuclear overhauser effect
nuclear overhauser enhancement spectroscopy
Protein Folding
Protein Structure, Tertiary
RMSD
root mean square deviation
Telethonin
Thermodynamics
Transcription Factors
α-Actinin
title Structure and dynamics of the human muscle LIM protein
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