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Structural insights into the interaction of human p97 N-terminal domain and SHP motif in Derlin-1 rhomboid pseudoprotease.
- Source :
-
FEBS Letters . Dec2016, Vol. 590 Issue 23, p4402-4413. 12p. - Publication Year :
- 2016
-
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 Å 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 590
- Issue :
- 23
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 121848889
- Full Text :
- https://doi.org/10.1002/1873-3468.12447