2boa

From Proteopedia

(Difference between revisions)

Revision as of 13:49, 13 December 2023

Human procarboxypeptidase A4.

Structural highlights

2boa is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBPA4_HUMAN Metalloprotease that could be involved in the histone hyperacetylation pathway.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI. Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells. Cancer Res. 1999 Jun 15;59(12):2981-8. PMID:10383164
↑ Garcia-Castellanos R, Bonet-Figueredo R, Pallares I, Ventura S, Aviles FX, Vendrell J, Gomis-Rutha FX. 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. 2005 Sep;62(17):1996-2014. PMID:16091843 doi:10.1007/s00018-005-5174-4

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2boa"

@@ Line 3: / Line 3: @@
 <StructureSection load='2boa' size='340' side='right'caption='[[2boa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2boa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BOA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2boa]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BOA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bo9|2bo9]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2boa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2boa OCA], [https://pdbe.org/2boa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2boa RCSB], [https://www.ebi.ac.uk/pdbsum/2boa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2boa ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CBPA4_HUMAN CBPA4_HUMAN] Metalloprotease that could be involved in the histone hyperacetylation pathway.<ref>PMID:10383164</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Aviles, F X]]
+[[Category: Aviles FX]]
-[[Category: Bonet-Figueredo, R]]
+[[Category: Bonet-Figueredo R]]
-[[Category: Garcia-Castellanos, R]]
+[[Category: Garcia-Castellanos R]]
-[[Category: Gomis-Ruth, F X]]
+[[Category: Gomis-Ruth FX]]
-[[Category: Pallares, I]]
+[[Category: Pallares I]]
-[[Category: Vendrell, J]]
+[[Category: Vendrell J]]
-[[Category: Ventura, S]]
+[[Category: Ventura S]]
-[[Category: Carboxypeptidase]]
-[[Category: Exopropeptidase]]
-[[Category: Hydrolase]]
-[[Category: Metalloprocarboxypeptidase]]
-[[Category: Metalloprotease]]
-[[Category: X-ray crystal structure]]
-[[Category: Zymogen]]

2boa

From Proteopedia

Revision as of 13:49, 13 December 2023

Human procarboxypeptidase A4.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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