Trimeric structure and flexibility of the L1ORF1 protein in human L1 retrotransposition

被引：0
|
作者：
Elena Khazina
Vincent Truffault
Regina Büttner
Steffen Schmidt
Murray Coles
Oliver Weichenrieder
机构：
[1] Max Planck Institute for Developmental Biology,Department of Biochemistry
[2] Max Planck Institute for Developmental Biology,Department of Protein Evolution
来源：
Nature Structural & Molecular Biology | 2011年 / 18卷
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摘要：
The process by which mammalian L1 retrotransposons move around the genome is not entirely clear. Now structural work on L1ORF1 protein, an RNA-binding protein essential for retrotransposition, reveals a trimeric organization and considerable interdomain flexibility. The latter is shown by mutagenesis to be critical for retrotransposition.
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页码：1006 / 1014
页数：8
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