5GLF: Structural insights into the interaction of p97 N-terminal domain and SHP motif in Derlin-1 rhomboid pseudoprotease

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 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 beta-strand that interacts with the beta-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.
PDB ID: 5GLFDownload
MMDB ID: 144689
PDB Deposition Date: 2016/7/11
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 2.25  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 5GLF: dimeric; determined by author and by software (PISA)
Molecular Components in 5GLF
Label Count Molecule
Proteins (2 molecules)
Transitional Endoplasmic Reticulum Atpase(Gene symbol: VCP)
Molecule annotation
Derlin-1(Gene symbol: DERL1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB