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Structural basis for the interaction between human Npl4 and Npl4-binding motif of human Ufd1
Thang Quyet Nguyen1, Le Thi My Le1, Do Hyeon Kim1
1Department of Chemistry, College of Natural Sciences, Soongsil University, Seoul 06978, Republic of Korea.
Structure (London, England : 1993)
|September 10, 2022
Summary
The human p97-Ufd1-Npl4 complex
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- The p97-Ufd1-Npl4 complex is a key cofactor for human p97 ATPase.
- This complex facilitates the translocation and degradation of ubiquitinated proteins.
- Structural data for the human complex was previously lacking.
Purpose of the Study:
- To determine the crystal structures of the human Ufd1-Npl4 (UN) complex and human Npl4 (hNpl4).
- To elucidate the atomic details and interactions within the human UN complex.
Main Methods:
- X-ray crystallography was used to determine the structures of hNpl4 and the human UN complex.
- Site-directed mutagenesis was employed to study protein-protein interactions.
Main Results:
- The crystal structures of the human UN complex at 2.7 Å and hNpl4 at 3.0 Å were determined.
- Atomic details of the interaction between hUfd1 and hNpl4 were revealed.
Conclusions:
- The study provides the first structural insights into the human UN complex.
- This structural information is crucial for understanding the mechanism of p97-mediated protein degradation.
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