Small-angle X-ray scattering reveals compact domain-domain interactions in the n-terminal region of filamin C
Sethi, R., & Ylänne, J. (2014). Small-angle X-ray scattering reveals compact domain-domain interactions in the n-terminal region of filamin C. PLoS ONE, 9(9), Article e107457. https://doi.org/10.1371/journal.pone.0107457
Published inPLoS ONE
© 2014 Sethi, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License.
Filamins are multi-domain, actin cross-linking, and scaffolding proteins. In addition to the actin cross-linking function, filamins have a role in mechanosensor signaling. The mechanosensor function is mediated by domain-domain interaction in the C-terminal region of filamins. Recently, we have shown that there is a three-domain interaction module in the Nterminal region of filamins, where the neighboring domains stabilize the structure of the middle domain and thereby regulate its interaction with ligands. In this study, we have used small-angle X-ray scattering as a tool to screen for potential domain-domain interactions in the N-terminal region. We found evidence of four domain-domain interactions with varying flexibility. These results confirm our previous study showing that domains 3, 4, and 5 exist as a compact three domain module. In addition, we report interactions between domains 11–12 and 14–15, which are thus new candidate sites for mechanical regulation.
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Except where otherwise noted, this item's license is described as © 2014 Sethi, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License.
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