Structural basis for C-degron selectivity across KLHDCX family E3 ubiquitin ligases
DC Scott, S Chittori, N Purser, MT King… - Nature …, 2024 - nature.com
Specificity of the ubiquitin-proteasome system depends on E3 ligase-substrate interactions.
Many such pairings depend on E3 ligases binding to peptide-like sequences-termed N-or C …
Many such pairings depend on E3 ligases binding to peptide-like sequences-termed N-or C …
Principles of paralog-specific targeted protein degradation engaging the C-degron E3 KLHDC2
DC Scott, S Dharuman, E Griffith, SC Chai… - Nature …, 2024 - nature.com
PROTAC®(proteolysis-targeting chimera) molecules induce proximity between an E3 ligase
and protein-of-interest (POI) to target the POI for ubiquitin-mediated degradation …
and protein-of-interest (POI) to target the POI for ubiquitin-mediated degradation …
How kelch domain-containing protein 3 distinguishes between the C-end degron of herpesviral protein UL49. 5 and its mutants–Insights from molecular dynamics
MJ Ślusarz - Bioorganic & Medicinal Chemistry, 2024 - Elsevier
The C-terminal residues of proteins can function as degrons recognized by ubiquitin ligases
for proteasomal degradation. Kelch domain-containing protein 3 (KLHDC3) is a substrate …
for proteasomal degradation. Kelch domain-containing protein 3 (KLHDC3) is a substrate …
An intrinsic network of polar interactions is responsible for binding of UL49.5 C‐degron by the CRL2KLHDC3 ubiquitin ligase
MJ Ślusarz, AD Lipińska - Proteins: Structure, Function, and …, 2024 - Wiley Online Library
Abstract Bovine herpesvirus type 1 (BoHV‐1) is a pathogen of cattle responsible for
infectious bovine rhinotracheitis. The BoHV‐1 UL49. 5 is a transmembrane protein that …
infectious bovine rhinotracheitis. The BoHV‐1 UL49. 5 is a transmembrane protein that …