Key result
The solution structure of chicken CRP1 determined by NMR spectroscopy reveals that its two LIM domains represent completely independent folding units with no apparent interactions.
Population
Chicken cysteine-rich protein, CRP1
Design
Preclinical
Authors
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Supports adapter role for CRP1 in muscle differentiation; leaves open translation to mammalian cardiac development.
The structural independence and spatial separation of the two LIM domains of CRP1 suggest an adapter or linker role for the protein in muscle differentiation.
Yao et al. (1999) studied this question. The solution structure of chicken CRP1 determined by NMR spectroscopy reveals that its two LIM domains represent completely independent folding units with no apparent interactions.
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