5n71 | pdb_00005n71

CRYSTAL STRUCTURE OF MATURE CATHEPSIN D FROM THE TICK IXODES RICINUS (IRCD1)

spinqualitylabelsall models 5n71, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n71 is a 1 chain structure with sequence from Common tick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PEG, SO4 Related: 5n70 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Pepsin-family aspartic peptidases are biosynthesized as inactive zymogens in which the propeptide blocks the active site until its proteolytic removal upon enzyme activation. Here, we describe a novel dual regulatory function for the propeptide using a set of crystal structures of the parasite cathepsin D IrCD1. In the IrCD1 zymogen, intramolecular autoinhibition by the intact propeptide is mediated by an evolutionarily conserved exosite on the enzyme core. After activation, the mature enzyme employs the same exosite to rebind a small fragment derived from the cleaved propeptide. This fragment functions as an effective natural inhibitor of mature IrCD1 that operates in a pH-dependent manner through a unique allosteric inhibition mechanism. The study uncovers the propeptide-binding exosite as a target for the regulation of pepsin-family aspartic peptidases and defines the structural requirements for exosite inhibition. Novel Structural Mechanism of Allosteric Regulation of Aspartic Peptidases via an Evolutionarily Conserved Exosite.,Hanova I, Brynda J, Houstecka R, Alam N, Sojka D, Kopacek P, Maresova L, Vondrasek J, Horn M, Schueler-Furman O, Mares M Cell Chem Biol. 2018 Jan 26. pii: S2451-9456(18)30001-1. doi:, 10.1016/j.chembiol.2018.01.001. PMID:29396291 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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