Crystallographic analysis of a pepstatin analogue binding to the aspartyl proteinase penicillopepsin at 1.8 angstroms resolution
Structure:
Protein (penicillopepsin). Chain: e. Synonym: peptidase a. Engineered: yes. Pepstatin analogue isovaleryl-val-val-sta-o-et. Chain: i. Engineered: yes
Source:
Penicillium janthinellum. Organism_taxid: 5079.
Resolution:
1.80Å
R-factor:
0.131
Authors:
A.R.Sielecki,M.N.G.James
Key ref:
M.N.G.James
et al.
(1983).
Crystallographic analysis of a pepstatin analogue binding to the aspartyl proteinase penicillopepsin at 1.8 angstroms resolution.
Peptides: structure and function, Proceedings of the of the eighth american peptide symposium,
1,
521.
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.