Journal
NATURE COMMUNICATIONS
Volume 10, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-019-11684-x
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Funding
- Korea Institute of Planning and Evaluation for Technology in Food, Agriculture, and Forestry (IPET
- ARC program) - Ministry of Agriculture, Food and Rural Affairs [710012-03-1-HD120]
- National Research Foundation of Korea [NRF-2017R1A2B2003992, NRF-2017M3A9R6029755, NRF-2016R1A2B2014493]
- BK21 Plus Program of the Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea
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Nuclear structure and function are governed by lamins, which are intermediate filaments that mostly consist of a-helices. Different lamin assembly models have been proposed based on low resolution and fragmented structures. However, their assembly mechanisms are still poorly understood at the molecular level. Here, we present the crystal structure of a long human lamin fragment at 3.2 angstrom resolution that allows the visualization of the features of the full-length protein. The structure shows an anti-parallel arrangement of the two coiled-coil dimers, which is important for the assembly process. We further discover an interaction between the lamin dimers by using chemical cross-linking and mass spectrometry analysis. Based on these two interactions, we propose a molecular mechanism for lamin assembly that is in agreement with a recent model representing the native state and could explain pathological mutations. Our findings also provide the molecular basis for assembly mechanisms of other intermediate filaments.
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