2boa

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[[Image:2boa.gif|left|200px]]<br /><applet load="2boa" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2boa.gif|left|200px]]
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caption="2boa, resolution 2.2&Aring;" />
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'''HUMAN PROCARBOXYPEPTIDASE A4.'''<br />
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{{Structure
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|PDB= 2boa |SIZE=350|CAPTION= <scene name='initialview01'>2boa</scene>, resolution 2.2&Aring;
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''HUMAN PROCARBOXYPEPTIDASE A4.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2BOA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOA OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16091843 16091843]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16091843 16091843]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zymogen]]
[[Category: zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:04:30 2008''

Revision as of 14:04, 20 March 2008

Image:2boa.gif


PDB ID 2boa

Drag the structure with the mouse to rotate
, resolution 2.2Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



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. 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

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