2boa
From Proteopedia
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| - | [[Image:2boa.gif|left|200px]]<br /><applet load="2boa" size=" | + | [[Image:2boa.gif|left|200px]]<br /><applet load="2boa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2boa, resolution 2.2Å" /> | caption="2boa, resolution 2.2Å" /> | ||
'''HUMAN PROCARBOXYPEPTIDASE A4.'''<br /> | '''HUMAN PROCARBOXYPEPTIDASE A4.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BOA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BOA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:26:17 2008'' |
Revision as of 08:26, 3 February 2008
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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 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.
About this Structure
2BOA is a Single protein structure of sequence from Homo sapiens with , and as ligands. Known structural/functional Site: . 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 Sun Feb 3 10:26:17 2008
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
