5YHU

Crystal structure of the DNA-binding domain of human myelin-gene regulatory factor

5YHU の概要

• エントリーDOI: 10.2210/pdb5yhu/pdb
• 分子名称: Myelin regulatory factor (2 entities in total)
• 機能のキーワード: myelingene regulatory factor, dna-binding domain, 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: 57704.99

構造登録者

Chen, B.,Zhu, Y.,Ye, S.,Zhang, R. (登録日: 2017-09-30, 公開日: 2018-05-23, 最終更新日: 2024-03-27)

主引用文献

Chen, B.,Zhu, Y.,Ye, S.,Zhang, R.
Structure of the DNA-binding domain of human myelin-gene regulatory factor reveals its potential protein-DNA recognition mode.
J. Struct. Biol., 203:170-178, 2018

PubMed Abstract: Myelin-gene regulatory factor (MYRF) is a membrane-bound transcription factors, which is responsible for the differentiation of oligodendrocytes and myelination of central nervous system. Followed by a self-cleavage by the intramolecular chaperone auto-processing (ICA) domain, DNA-binding domain (DBD) of MYRF is released from the endoplasmic reticulum (ER) and was then translocated to the nucleus to regulate gene expression. In present work, we have solved the crystal structure of the human MYRF-DBD to 1.85-Å resolution. It exhibits a typical s-type Ig-fold and packs as symmetric trimeric form in the crystal via hydrogen-bond networks in three regions. Accordingly, we identified a couple of key residues on MYRF-DBD, which might play important roles in DNA-binding, in particular Arg521 on its C-terminal tail. The R521A mutant of DBD showed only 17% affinity to dsDNA targets compared to wild-type DBD. Then we built a plausible protein-DNA binding model of MYRF-DBD, which will help to elucidate its mechanism in DNA-binding and transcriptional regulation.

PubMed: 29729323
DOI: 10.1016/j.jsb.2018.04.007

実験手法

X-RAY DIFFRACTION (1.85 Å)