3LKX

Human nac dimerization domain

3LKX の概要

• エントリーDOI: 10.2210/pdb3lkx/pdb
• 分子名称: Transcription factor BTF3, Nascent polypeptide-associated complex subunit alpha (3 entities in total)
• 機能のキーワード: beta-barrel, chaperone
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm : P20290 Q13765
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13137.83

構造登録者

Liu, Y.,Hu, Y.,Li, X.,Niu, L.,Teng, M. (登録日: 2010-01-28, 公開日: 2010-03-23, 最終更新日: 2023-11-01)

主引用文献

Liu, Y.,Hu, Y.,Li, X.,Niu, L.,Teng, M.
The crystal structure of the human nascent polypeptide-associated complex domain reveals a nucleic acid-binding region on the NACA subunit
Biochemistry, 49:2890-2896, 2010

PubMed Abstract: In archaea and eukaryotes, the nascent polypeptide-associated complex (NAC) is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes. The eukaryotic NAC is a heterodimer, and its two subunits form a stable complex through a dimerizing domain called the NAC domain. In addition to acting as a protein translation chaperone, the NAC subunits also function individually in transcriptional regulation. Here we report the crystal structure of the human NAC domain, which reveals the manner of human NAC dimerization. On the basis of the structure, we identified a region in the NAC domain of the human NAC alpha-subunit as a new nucleic acid-binding region, which is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit.

PubMed: 20214399
DOI: 10.1021/bi902050p

実験手法

X-RAY DIFFRACTION (2.5 Å)