Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.

ABSTRACT: The integral membrane protein zinc metalloprotease ZMPSTE24 possesses a completely novel structure, comprising seven long kinked transmembrane helices that encircle a voluminous 14 000 ų cavity within the membrane. Functionally conserved soluble zinc metalloprotease residues are contained within this cavity. As part of an effort to understand the structural and functional relationships between ZMPSTE24 and soluble zinc metalloproteases, the inhibition of ZMPSTE24 by phosphoramidon [N-(α-rhamnopyranosyl-oxyhydroxyphosphinyl)-Leu-Trp], a transition-state analog and competitive inhibitor of multiple soluble zinc metalloproteases, especially gluzincins, has been characterized functionally and structurally. The functional results, the determination of preliminary IC₅₀ val

SUBMITTER: Goblirsch BR 

PROVIDER: S-EPMC6079626 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature