Structural insights into the interaction of human p97 N-terminal domain and SHP motif in Derlin-1 rhomboid pseudoprotease
| Autor: | Kyoung Ryoung Park, Jia Jia Lim, Tue Tu Ly, Jung Youn Kang, So Young Yoon, Jin Kuk Yang, Youngsoo Jun, Hyung-Seop Youn, Youngjin Lee, Jung-Gyu Lee, Soo Hyun Eom, Tae Gyun Kim, Jun Yop An |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amino Acid Motifs Biophysics Binding pocket Endoplasmic-reticulum-associated protein degradation Biology Antiparallel (biochemistry) Biochemistry 03 medical and health sciences Protein Domains Structural Biology Genetics Humans Amino Acid Sequence Molecular Biology Conserved Sequence Adenosine Triphosphatases Binding Sites Endoplasmic reticulum Rhomboid Membrane Proteins Nuclear Proteins Signal transducing adaptor protein Endoplasmic Reticulum-Associated Degradation Cell Biology Cell biology Crystallography 030104 developmental biology Motif (music) Apoproteins Protein Binding |
| Zdroj: | FEBS Letters. 590:4402-4413 |
| ISSN: | 0014-5793 |
| DOI: | 10.1002/1873-3468.12447 |
| Popis: | The interaction of the rhomboid pseudoprotease Derlin-1 and p97 is crucial for the retrotranslocation of polyubiquitinated substrates in the endoplasmic reticulum-associated degradation (ERAD) pathway. We report a 2.25 A resolution structure of the p97 N-terminal domain (p97N) in complex with the Derlin-1 SHP motif. Remarkably, the SHP motif adopts a short, antiparallel β-strand that interacts with the β-sheet of p97N–a site distinct from that to which most p97 adaptor proteins bind. Mutational and biochemical analyses contributed to defining the specific interaction, demonstrating the importance of a highly conserved binding pocket on p97N and a signature motif on SHP. Our findings may also provide insights into the interactions between other SHP-containing proteins and p97N. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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