Journal
FEBS LETTERS
Volume 590, Issue 18, Pages 3098-3110Publisher
WILEY
DOI: 10.1002/1873-3468.12362
Keywords
circular dichroism; recombinant proteins; SEC-MALLS; small-angle X-ray scattering; X-ray crystallography
Funding
- British Heart Foundation [PG/13/21/3007]
- Leducq Foundation [TNE-13CVD04]
- European Commission [656636]
- Marie Curie Actions (MSCA) [656636] Funding Source: Marie Curie Actions (MSCA)
Ask authors/readers for more resources
The cardiac ankyrin repeat protein (CARP) is up-regulated in the myocardium during cardiovascular disease and in response to mechanical or toxic stress. Stress-induced CARP interacts with the N2A spring region of the titin filament to modulate muscle compliance. We characterize the interaction between CARP and titin-N2A and show that the binding site in titin spans the dual domain UN2A-Ig81. We find that the unique sequence UN2A is not structurally disordered, but that it has a stable, elongated -helical fold that possibly acts as a constant force spring. Our findings portray CARP/titin-N2A as a structured node and help to rationalize the molecular basis of CARP mechanosensing in the sarcomeric I-band.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available