4lp9

Publication Abstract from PubMed

Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC50 = 0.62 microM) based on a reduced-bond transition-state inhibitor of mucorpepsin was co-crystallized with endothiapepsin and the crystal structure of the enzyme-inhibitor complex was determined at 1.35 A resolution. A total of 12 hydrogen bonds between the inhibitor and the active-site residues were identified. The resulting structure demonstrates a number of novel subsite interactions in the active-site cleft.

The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 A resolution.,Guo J, Cooper JB, Wood SP Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):30-3. doi:, 10.1107/S2053230X13032974. Epub 2013 Dec 24. PMID:24419612^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.