Structural insights into the interaction of human p97 N-terminal domain and SHP motif in Derlin-1 rhomboid pseudoprotease
- Authors
- Lim, Jia Jia; Lee, Youngjin; Yoon, So Young; Ly, Tue Tu; Kang, Jung Youn; Youn, Hyung-Seop; An, Jun Yop; Lee, Jung-Gyu; Park, Kyoung Ryoung; Kim, Tae Gyun; Yang, Jin Kuk; Jun, Youngsoo; Eom, Soo Hyun
- Issue Date
- Dec-2016
- Publisher
- WILEY-BLACKWELL
- Keywords
- crystal structure; Derlin-1; endoplasmic reticulum-associated degradation; p97; SHP motif
- Citation
- FEBS LETTERS, v.590, no.23, pp.4402 - 4413
- Journal Title
- FEBS LETTERS
- Volume
- 590
- Number
- 23
- Start Page
- 4402
- End Page
- 4413
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/7434
- DOI
- 10.1002/1873-3468.12447
- ISSN
- 0014-5793
- Abstract
- The interaction of the rhomboid pseudoprotease Derlin-1 and p97 is crucial for the retrotranslocation of polyubiquitinated substrates in the endoplasmic reticulum-associated degradation pathway. We report a 2.25 angstrom 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 -strand that interacts with the -sheet of p97Na 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.
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Collections - College of Natural Sciences > Department of Chemistry > 1. Journal Articles
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