原创力文档structural basis of the chromodomain of cbx3 bound to methylated peptides from histone h1 and g9a结构基础的chromodomain cbx3必将从组蛋白甲基化肽g9a h1和.pdfVIP
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structural basis of the chromodomain of cbx3 bound to methylated peptides from histone h1 and g9a结构基础的chromodomain cbx3必将从组蛋白甲基化肽g9a h1和
Structural Basis of the Chromodomain of Cbx3 Bound to
Methylated Peptides from Histone H1 and G9a
1,2. 3. 3 3 3 3,4
Jianbin Ruan , Hui Ouyang , Maria F. Amaya , Mani Ravichandran , Peter Loppnau , Jinrong Min *,
Jianye Zang1,2*
1 Hefei National Laboratory for Physical Sciences, Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People’s Republic of
China, 2 Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, People’s Republic of China, 3 Structural Genomics Consortium, University of
Toronto, Toronto, Ontario, Canada, 4 Department of Physiology, University of Toronto, Toronto, Ontario, Canada
Abstract
Background: HP1 proteins are highly conserved heterochromatin proteins, which have been identified to be structural
adapters assembling a variety of macromolecular complexes involved in regulation of gene expression, chromatin
remodeling and heterochromatin formation. Much evidence shows that HP1 proteins interact with numerous proteins
including methylated histones, histone methyltransferases and so on. Cbx3 is one of the paralogues of HP1 proteins, which
has been reported to specifically recognize trimethylated histone H3K9 mark, and a consensus binding motif has been
defined for the Cbx3 chromodomain.
Methodology/Principal Findings: Here, we found that the Cbx3 chromodomain can bind to H1K26me2 and G9aK185me3
with comparable binding affinities compared to H3K9me3. We also determined the crystal structures of the human Cbx3
ch
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