2pjh

From Proteopedia

Revision as of 10:33, 23 January 2008

Strctural Model of the p97 N domain- npl4 UBD complex

Overview

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.

About this Structure

2PJH is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Detailed structural insights into the p97-Npl4-Ufd1 interface., Isaacson RL, Pye VE, Simpson P, Meyer HH, Zhang X, Freemont PS, Matthews S, J Biol Chem. 2007 Jul 20;282(29):21361-9. Epub 2007 May 9. PMID:17491009

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