2PJH

Strctural Model of the p97 N domain- npl4 UBD complex

2PJH の概要

• エントリーDOI: 10.2210/pdb2pjh/pdb
• 分子名称: Nuclear protein localization protein 4 homolog, Transitional endoplasmic reticulum ATPase (2 entities in total)
• 機能のキーワード: p97, ufd1, npl4, aaa, atpase, protein binding, transport protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Cytoplasm, cytosol (By similarity): P60670; Cytoplasm, cytosol: Q01853
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30891.54

構造登録者

Isaacson, R.,Pye, V.E.,Simpson, S.,Meyer, H.H.,Zhang, X.,Freemont, P. (登録日: 2007-04-16, 公開日: 2007-05-08, 最終更新日: 2024-05-22)

主引用文献

Isaacson, R.L.,Pye, V.E.,Simpson, P.,Meyer, H.H.,Zhang, X.,Freemont, P.S.,Matthews, S.
Detailed structural insights into the p97-Npl4-Ufd1 interface.
J.Biol.Chem., 282:21361-21369, 2007

PubMed Abstract: The AAA ATPase, p97, achieves its versatility through binding to a wide range of cofactor proteins that adapt it to different cellular functions. The heterodimer UN (comprising Ufd1 and Npl4) is an adaptor complex that recruits p97 for numerous tasks, many of which involve the ubiquitin pathway. Insights into the structural specificity of p97 for its UN adaptor are currently negligible. Here, we present the solution structure of the Npl4 "ubiquitin-like" domain (UBD), which adopts a beta-grasp fold with a 3(10) helical insert. Moreover we performed a chemical shift perturbation analysis of its binding surface with the p97 N domain. We assigned the backbone amides of the p97 N domain and probed both its reciprocal binding surface with Npl4 UBD and its interaction with the p97-binding region of Ufd1. NMR data recorded on a 400-kDa full-length UN-hexamer p97 complex reveals an identical mode of interaction. We calculated a structural model for the p97 N-Npl4 UBD complex, and a comparison with the p97-p47 adaptor complex reveals subtle differences in p97 adaptor recognition and specificity.

PubMed: 17491009
DOI: 10.1074/jbc.M610069200

実験手法

SOLUTION NMR