6ANO

Crystal structure of human FLASH N-terminal domain

6ANO の概要

• エントリーDOI: 10.2210/pdb6ano/pdb
• 分子名称: CASP8-associated protein 2 (2 entities in total)
• 機能のキーワード: coiled-coil, gene regulation
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: Q9UKL3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23045.17

構造登録者

Aik, W.S.,Tong, L. (登録日: 2017-08-14, 公開日: 2017-11-15, 最終更新日: 2024-10-23)

主引用文献

Aik, W.S.,Lin, M.H.,Tan, D.,Tripathy, A.,Marzluff, W.F.,Dominski, Z.,Chou, C.Y.,Tong, L.
The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing.
PLoS ONE, 12:e0186034-e0186034, 2017

PubMed Abstract: Unlike canonical pre-mRNAs, animal replication-dependent histone pre-mRNAs lack introns and are processed at the 3'-end by a mechanism distinct from cleavage and polyadenylation. They have a 3' stem loop and histone downstream element (HDE) that are recognized by stem-loop binding protein (SLBP) and U7 snRNP, respectively. The N-terminal domain (NTD) of Lsm11, a component of U7 snRNP, interacts with FLASH NTD and these two proteins recruit the histone cleavage complex containing the CPSF-73 endonuclease for the cleavage reaction. Here, we determined crystal structures of FLASH NTD and found that it forms a coiled-coil dimer. Using solution light scattering, we characterized the stoichiometry of the FLASH NTD-Lsm11 NTD complex and found that it is a 2:1 heterotrimer, which is supported by observations from analytical ultracentrifugation and crosslinking.

PubMed: 29020104
DOI: 10.1371/journal.pone.0186034

実験手法

X-RAY DIFFRACTION (2.61 Å)