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==Human carboxypeptidase A4 in complex with human latexin.==
==Human carboxypeptidase A4 in complex with human latexin.==
<StructureSection load='2bo9' size='340' side='right' caption='[[2bo9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='2bo9' size='340' side='right'caption='[[2bo9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bo9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bk7 2bk7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BO9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bo9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bk7 2bk7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BO9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</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]] 1.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2boa|2boa]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo9 OCA], [http://pdbe.org/2bo9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bo9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bo9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bo9 ProSAT]</span></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=2bo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo9 OCA], [https://pdbe.org/2bo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bo9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bo9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CBPA4_HUMAN CBPA4_HUMAN]] Metalloprotease that could be involved in the histone hyperacetylation pathway.<ref>PMID:10383164</ref> [[http://www.uniprot.org/uniprot/LXN_HUMAN LXN_HUMAN]] Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4. May play a role in inflammation.<ref>PMID:15738388</ref> 
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bo9 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bo9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The only endogenous protein inhibitor known for metallocarboxypeptidases (MCPs) is latexin, a 25-kDa protein discovered in the rat brain. Latexin, alias endogenous carboxypeptidase inhibitor, inhibits human CPA4 (hCPA4), whose expression is induced in prostate cancer cells after treatment with histone deacetylase inhibitors. hCPA4 is a member of the A/B subfamily of MCPs and displays the characteristic alpha/beta-hydrolase fold. Human latexin consists of two topologically equivalent subdomains, reminiscent of cystatins, consisting of an alpha-helix enveloped by a curved beta-sheet. These subdomains are packed against each other through the helices and linked by a connecting segment encompassing a third alpha-helix. The enzyme is bound at the interface of these subdomains. The complex occludes a large contact surface but makes rather few contacts, despite a nanomolar inhibition constant. This low specificity explains the flexibility of latexin in inhibiting all vertebrate A/B MCPs tested, even across species barriers. In contrast, modeling studies reveal why the N/E subfamily of MCPs and invertebrate A/B MCPs are not inhibited. Major differences in the loop segments shaping the border of the funnel-like access to the protease active site impede complex formation with latexin. Several sequences ascribable to diverse tissues and organs have been identified in vertebrate genomes as being highly similar to latexin. They are proposed to constitute the latexin family of potential inhibitors. Because they are ubiquitous, latexins could represent for vertebrate A/B MCPs the counterparts of tissue inhibitors of metalloproteases for matrix metalloproteinases.
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin.,Pallares I, Bonet R, Garcia-Castellanos R, Ventura S, Aviles FX, Vendrell J, Gomis-Ruth FX Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3978-83. Epub 2005 Feb 28. PMID:15738388<ref>PMID:15738388</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bo9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Carboxypeptidase|Carboxypeptidase]]
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Aviles, F X]]
[[Category: Large Structures]]
[[Category: Bonet, R]]
[[Category: Aviles FX]]
[[Category: Garcia-Castellanos, R]]
[[Category: Bonet R]]
[[Category: Gomis-Rueth, F X]]
[[Category: Garcia-Castellanos R]]
[[Category: Pallares, I]]
[[Category: Gomis-Rueth FX]]
[[Category: Vendrell, J]]
[[Category: Pallares I]]
[[Category: Ventura, S]]
[[Category: Vendrell J]]
[[Category: Endogenous protein inhibitor]]
[[Category: Ventura S]]
[[Category: Hydrolase]]
[[Category: Latexin]]
[[Category: Metallocarboxypeptidase]]
[[Category: Metalloprotease carboxypeptidase]]
[[Category: X-ray crystal structure]]

Latest revision as of 09:38, 1 May 2024

Human carboxypeptidase A4 in complex with human latexin.Human carboxypeptidase A4 in complex with human latexin.

Structural highlights

2bo9 is a 4 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2bk7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
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.

See Also

References

  1. ↑ 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

2bo9, resolution 1.60Å

Drag the structure with the mouse to rotate

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OCA
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