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伴侣蛋白Chz1与组蛋白H2A.Z-H2B复合的核磁共振结构。

NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.

作者信息

Zhou Zheng, Feng Hanqiao, Hansen D Flemming, Kato Hidenori, Luk Ed, Freedberg Daron I, Kay Lewis E, Wu Carl, Bai Yawen

机构信息

Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.

出版信息

Nat Struct Mol Biol. 2008 Aug;15(8):868-9. doi: 10.1038/nsmb.1465. Epub 2008 Jul 20.

Abstract

The NMR structure of budding yeast chaperone Chz1 complexed with histones H2A.Z-H2B has been determined. Chz1 forms a long irregular chain capped by two short alpha-helices, and uses both positively and negatively charged residues to stabilize the histone dimer. A molecular model that docks Chz1 onto the nucleosome has implications for its potential functions.

摘要

已确定与组蛋白H2A.Z-H2B复合的出芽酵母伴侣蛋白Chz1的核磁共振结构。Chz1形成一条由两个短α螺旋封端的长不规则链,并利用带正电和带负电的残基来稳定组蛋白二聚体。将Chz1对接至核小体上的分子模型对其潜在功能具有启示意义。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/575a/2574748/f7d38eecd729/nihms59985f1.jpg

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