2W2H

Structural basis of transcription activation by the Cyclin T1-Tat-TAR RNA complex from EIAV

2W2H の概要

• エントリーDOI: 10.2210/pdb2w2h/pdb
• 分子名称: CYCLIN-T1, PROTEIN TAT, 5'-R(*GP*CP*UP*CP*AP*GP*AP*UP*CP*UP *GP*CP*GP*GP*UP*CP*UP*GP*AP*GP*C)-3', ... (5 entities in total)
• 機能のキーワード: rna-binding protein, tar, tat, cyclin, nucleus, activator, cyclin t1, host-virus interaction, transcription regulation, cell cycle, rna-binding, acetylation, coiled coil, transcription, cell division, crystallization, rna binding protein
• 由来する生物種: EQUUS CABALLUS (HORSE); 詳細
• 細胞内の位置: Nucleus (By similarity): Q9XT26; Host nucleus, host nucleolus (By similarity): P20920
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 82837.14

構造登録者

Anand, K.,Geyer, M. (登録日: 2008-10-30, 公開日: 2008-12-09, 最終更新日: 2023-12-13)

主引用文献

Anand, K.,Schulte, A.,Vogel-Bachmayr, K.,Scheffzek, K.,Geyer, M.
Structural Insights Into the Cyclin T1-Tat-Tar RNA Transcription Activation Complex from Eiav.
Nat.Struct.Mol.Biol., 15:1287-, 2008

PubMed Abstract: The replication of many retroviruses is mediated by a transcriptional activator protein, Tat, which activates RNA polymerase II at the level of transcription elongation. Tat interacts with Cyclin T1 of the positive transcription-elongation factor P-TEFb to recruit the transactivation-response TAR RNA, which acts as a promoter element in the transcribed 5' end of the viral long terminal repeat. Here we present the structure of the cyclin box domain of Cyclin T1 in complex with the Tat protein from the equine infectious anemia virus and its corresponding TAR RNA. The basic RNA-recognition motif of Tat adopts a helical structure whose flanking regions interact with a cyclin T-specific loop in the first cyclin box repeat. Together, both proteins coordinate the stem-loop structure of TAR. Our findings show that Tat binds to a surface on Cyclin T1 similar to where recognition motifs from substrate and inhibitor peptides were previously found to interact within Cdk-cyclin pairs.

PubMed: 19029897
DOI: 10.1038/NSMB.1513

実験手法

X-RAY DIFFRACTION (3.25 Å)