3S6W

Crystal structure of Tudor domain of human TDRD3

3S6W の概要

• エントリーDOI: 10.2210/pdb3s6w/pdb
• 分子名称: Tudor domain-containing protein 3, ISOPROPYL ALCOHOL (3 entities in total)
• 機能のキーワード: tudor, methylated arginine recognize, iso-propanol, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : Q9H7E2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6445.35

構造登録者

Liu, H.P.,Xu, R.M. (登録日: 2011-05-26, 公開日: 2012-03-07, 最終更新日: 2023-11-01)

主引用文献

Liu, K.,Guo, Y.H.,Liu, H.P.,Bian, C.B.,Lam, R.,Liu, Y.,Mackenzie, F.,Rojas, L.A.,Reinberg, D.,Bedford, M.T.,Xu, R.M.,Min, J.R.
Crystal structure of TDRD3 and methyl-arginine binding characterization of TDRD3, SMN and SPF30
Plos One, 7:e30375-e30375, 2012

PubMed Abstract: SMN (Survival motor neuron protein) was characterized as a dimethyl-arginine binding protein over ten years ago. TDRD3 (Tudor domain-containing protein 3) and SPF30 (Splicing factor 30 kDa) were found to bind to various methyl-arginine proteins including Sm proteins as well later on. Recently, TDRD3 was shown to be a transcriptional coactivator, and its transcriptional activity is dependent on its ability to bind arginine-methylated histone marks. In this study, we systematically characterized the binding specificity and affinity of the Tudor domains of these three proteins quantitatively. Our results show that TDRD3 preferentially recognizes asymmetrical dimethylated arginine mark, and SMN is a very promiscuous effector molecule, which recognizes different arginine containing sequence motifs and preferentially binds symmetrical dimethylated arginine. SPF30 is the weakest methyl-arginine binder, which only binds the GAR motif sequences in our library. In addition, we also reported high-resolution crystal structures of the Tudor domain of TDRD3 in complex with two small molecules, which occupy the aromatic cage of TDRD3.

PubMed: 22363433
DOI: 10.1371/journal.pone.0030375

実験手法

X-RAY DIFFRACTION (1.78 Å)