2boa
From Proteopedia
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HUMAN PROCARBOXYPEPTIDASE A4.
Overview
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 ... [(full description)]
About this Structure
2BOA is a [Single protein] structure of sequence from [Homo sapiens] with NAG, ZN and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the endogenous inhibitor latexin., Garcia-Castellanos R, Bonet-Figueredo R, Pallares I, Ventura S, Aviles FX, Vendrell J, Gomis-Rutha FX, Cell Mol Life Sci. 2005 Sep;62(17):1996-2014. PMID:16091843
Page seeded by OCA on Tue Oct 30 08:23:52 2007
Categories: Homo sapiens | Single protein | Aviles, F.X. | Bonet-Figueredo, R. | Garcia-Castellanos, R. | Gomis-Ruth, F.X. | Pallares, I. | Vendrell, J. | Ventura, S. | GOL | NAG | ZN | Carboxypeptidase | Exopropeptidase | Hydrolase | Metalloprocarboxypeptidase | Metalloprotease | X-ray crystal structure | Zymogen