ArticleActa crystallographica. Section D, Structural biology2026
Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.
Article in Acta crystallographica. Section D, Structural biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Nucleosomes are the repeating unit of chromatin. They act as recognition platforms for chromatin-binding factors that coordinate genome maintenance. The chromatin remodeler Amplified in Liver Cancer 1 (ALC1) is a key component of the DNA-damage response and a promising therapeutic target in cancer. Through extensive classification of our previously deposited cryo-electron microscopy dataset, we identified a previously unresolved ALC1-nucleosome complex characterized by a more open conformation of ALC1. This is the first structure of ALC1 in which all domains are visualized in the context of a nucleosome complex, including the regulatory macro domain and a single α-helix motif within the linker. This newly identified conformation may represent an intermediate between the auto-inhibited and active states, and provides new structural insights into the conformational transitions that regulate the activity of ALC1.
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