5J39

Crystal Structure of the extended TUDOR domain from TDRD2

5J39 の概要

• エントリーDOI: 10.2210/pdb5j39/pdb
• 分子名称: Tudor and KH domain-containing protein, CACODYLATE ION, UNKNOWN ATOM OR ION, ... (4 entities in total)
• 機能のキーワード: tudor domain, structural genomics consortium, sgc, transcription
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47536.65

構造登録者

Zhang, H.,Tempel, W.,Dong, A.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2016-03-30, 公開日: 2016-04-13, 最終更新日: 2023-09-27)

主引用文献

Zhang, H.,Liu, K.,Izumi, N.,Huang, H.,Ding, D.,Ni, Z.,Sidhu, S.S.,Chen, C.,Tomari, Y.,Min, J.
Structural basis for arginine methylation-independent recognition of PIWIL1 by TDRD2.
Proc. Natl. Acad. Sci. U.S.A., 114:12483-12488, 2017

PubMed Abstract: The P-element-induced wimpy testis (PIWI)-interacting RNA (piRNA) pathway plays a central role in transposon silencing and genome protection in the animal germline. A family of Tudor domain proteins regulates the piRNA pathway through direct Tudor domain-PIWI interactions. Tudor domains are known to fulfill this function by binding to methylated PIWI proteins in an arginine methylation-dependent manner. Here, we report a mechanism of methylation-independent Tudor domain-PIWI interaction. Unlike most other Tudor domains, the extended Tudor domain of mammalian Tudor domain-containing protein 2 (TDRD2) preferentially recognizes an unmethylated arginine-rich sequence from PIWI-like protein 1 (PIWIL1). Structural studies reveal an unexpected Tudor domain-binding mode for the PIWIL1 sequence in which the interface of Tudor and staphylococcal nuclease domains is primarily responsible for PIWIL1 peptide recognition. Mutations disrupting the TDRD2-PIWIL1 interaction compromise piRNA maturation via 3'-end trimming in vitro. Our work presented here reveals the molecular divergence of the interactions between different Tudor domain proteins and PIWI proteins.

PubMed: 29118143
DOI: 10.1073/pnas.1711486114

実験手法

X-RAY DIFFRACTION (1.95 Å)