Structural basis for substrate selectivity by site-one protease revealed by studies with a small-molecule inhibitor

Site-one protease (S1P) carries out the first proteolytic step to activate membrane-bound effector proteins in the Golgi. S1P matures through an autocatalytic process that begins in the endoplasmic reticulum (ER) and culminates with the displacement of its inhibitory pro-domain by its cofactor, ster...

Celý popis

Uloženo v:

Podrobná bibliografie
Vydáno v:	Proceedings of the National Academy of Sciences - PNAS Ročník 122; číslo 18; s. e2426931122
Hlavní autoři:	Bullington, Ashley V, Micallo, Ilaria, Bajaj, Bilkish, Kumar, Pankaj, Schlamowitz, Netanya, Silva, Aurora, Hendrix, Sebastian, Zelcer, Noam, Kober, Daniel L
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 06.05.2025
Témata:	Crystallography, X-Ray Endoplasmic Reticulum - metabolism Humans Models, Molecular Proprotein Convertases - antagonists & inhibitors Proprotein Convertases - chemistry Proprotein Convertases - genetics Proprotein Convertases - metabolism Protein Binding Proteolysis Serine Endopeptidases - chemistry Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Substrate Specificity cholesterol SPRING site-1-protease cryo-EM proteases
ISSN:	1091-6490, 1091-6490
On-line přístup:	Zjistit podrobnosti o přístupu
Tagy:	Přidat tag Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!

Buďte první, kdo okomentuje tento záznam!