Back to search

Article

Structure of E3 ligase E6AP with a novel proteasome-binding site provided by substrate receptor hRpn10

2019-10-09

Abstract excerpt

Regulated proteolysis by the proteasome involves ∼800 enzymes for substrate modification with ubiquitin, of which ∼600 are E3 ligases. We report here that E6AP/UBE3A is distinguished from other ubiquitin E3 ligases by having a 12 nM binding site at the proteasome contributed by substrate receptor hRpn10/PSMD4/S5a. Intrinsically disordered by itself, and previously uncharacterized, this domain in hRpn10 locks into...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
5ca2dbab-e783-59a3-8986-3720e3ffe066
DOI
10.1101/797027
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Structure of E3 ligase E6AP with a novel proteasome-binding site provided by substrate receptor hRpn10DOI 10.1101/797027
Select a neighboring publication to make it the new centre.