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Structure and dynamics of the human muscle LIM protein
- Source :
- FEBS Letters
- Publication Year :
- 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.
- Subjects :
- Models, Molecular
Protein Folding
Telethonin
LIM-Homeodomain Proteins
Biophysics
Muscle Proteins
Biochemistry
DNA-binding protein
Cysteine rich protein
Avian Proteins
Structural Biology
Genetics
Animals
Humans
Eye Proteins
Molecular Biology
Nuclear Magnetic Resonance, Biomolecular
LIM domain
Adaptor Proteins, Signal Transducing
Homeodomain Proteins
Chemistry
Myogenesis
Membrane Proteins
α-Actinin
Cell Biology
LIM Domain Proteins
NMR
Cell biology
Protein Structure, Tertiary
DNA-Binding Proteins
Membrane protein
Thermodynamics
Protein folding
Myofibril
LHX3
Carrier Proteins
Transcription Factors
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....24a0dcc352d4df26cf1aab5be02f6820