2PJH
Strctural Model of the p97 N domain- npl4 UBD complex
Summary for 2PJH
| Entry DOI | 10.2210/pdb2pjh/pdb |
| Descriptor | Nuclear protein localization protein 4 homolog, Transitional endoplasmic reticulum ATPase (2 entities in total) |
| Functional Keywords | p97, ufd1, npl4, aaa, atpase, protein binding, transport protein |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Cytoplasm, cytosol (By similarity): P60670 Cytoplasm, cytosol: Q01853 |
| Total number of polymer chains | 2 |
| Total formula weight | 30891.54 |
| Authors | Isaacson, R.,Pye, V.E.,Simpson, S.,Meyer, H.H.,Zhang, X.,Freemont, P. (deposition date: 2007-04-16, release date: 2007-05-08, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 17491009DOI: 10.1074/jbc.M610069200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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