2BOA

Human procarboxypeptidase A4.

Summary for 2BOA

• Entry DOI: 10.2210/pdb2boa/pdb
• Related: 2BO9
• Descriptor: CARBOXYPEPTIDASE A4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: metalloprocarboxypeptidase, x-ray crystal structure, zymogen, metalloprotease, exopropeptidase, hydrolase, carboxypeptidase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Secreted : Q9UI42
• Total number of polymer chains: 2
• Total formula weight: 92370.65

Authors

Garcia-Castellanos, R.,Bonet-Figueredo, R.,Pallares, I.,Ventura, S.,Aviles, F.X.,Vendrell, J.,Gomis-Ruth, F.X. (deposition date: 2005-04-08, release date: 2005-12-13, Last modification date: 2024-10-16)

Primary citation

Garcia-Castellanos, R.,Bonet-Figueredo, R.,Pallares, I.,Ventura, S.,Aviles, F.X.,Vendrell, J.,Gomis-Ruth, F.X.
Detailed Molecular Comparison between the Inhibition Mode of A/B-Type Carboxypeptidases in the Zymogen State and by the Endogenous Inhibitor Latexin.
Cell.Mol.Life Sci., 62:1996-, 2005

PubMed Abstract: Treatment of advanced stages of prostate carcinoma with histone-deacetylase inhibitors entails expression of human procarboxypeptidase-A4 (hPCPA4). The three-dimensional structure of hPCPA4 has been solved and shows the features of related metallocarboxypeptidase zymogens, with a preformed alpha/beta/-hydrolase active-enzyme moiety (hCPA4) and an inhibiting pro-domain (PD). The protease moiety recalls a sphere, out of which a spherical cone has been cut. This results in a funnel-like structure, at the bottom of which the active-site cleft resides. The border of this funnel is shaped by loops, which are responsible for the interaction with the PD, characterised by a large interface area and relatively few contacts. Such an inhibitory mode is evocative of the recently reported structure of the human inhibitor latexin in its complex with hCPA4. The main contacting structure of latexin is similar to the one employed for PD inhibition. In both cases, active-site blocking relies mainly on a loop provided by the central part of a beta sheet.

PubMed: 16091843
DOI: 10.1007/S00018-005-5174-4

Experimental method

X-RAY DIFFRACTION (2.2 Å)