3MCB

Crystal structure of NAC domains of human nascent polypeptide-associated complex (NAC)

3MCB の概要

• エントリーDOI: 10.2210/pdb3mcb/pdb
• 関連するPDBエントリー: 3MCE
• 分子名称: Nascent polypeptide-associated complex subunit alpha, Transcription factor BTF3, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: beta-barrel like structure, nac, heterodimer, chaperone
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q13765 P20290
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12720.86

構造登録者

Wang, L.F.,Zhang, W.C.,Wang, L.,Zhang, X.J.C.,Li, X.M.,Rao, Z. (登録日: 2010-03-29, 公開日: 2010-07-14, 最終更新日: 2024-03-20)

主引用文献

Wang, L.F.,Zhang, W.C.,Wang, L.,Zhang, X.J.C.,Li, X.M.,Rao, Z.
Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit
Protein Cell, 1:406-416, 2010

PubMed Abstract: Nascent polypeptide associated complex (NAC) and its two isolated subunits, αNAC and βNAC, play important roles in nascent peptide targeting. We determined a 1.9 Å resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 Å resolution crystal structure of αNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and αNAC homodimerization. We found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a βNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC.

PubMed: 21203952
DOI: 10.1007/s13238-010-0049-3

実験手法

X-RAY DIFFRACTION (1.9 Å)