This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2bo9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:38, 1 May 2024) (edit) (undo)
 
(20 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2bo9.gif|left|200px]]<br />
 
-
<applet load="2bo9" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2bo9, resolution 1.60&Aring;" />
 
-
'''HUMAN CARBOXYPEPTIDASE A4 IN COMPLEX WITH HUMAN LATEXIN.'''<br />
 
-
==Overview==
+
==Human carboxypeptidase A4 in complex with human latexin.==
-
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.
+
<StructureSection load='2bo9' size='340' side='right'caption='[[2bo9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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='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='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'>[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>
 +
== 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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/2bo9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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>
-
==About this Structure==
+
==See Also==
-
2BO9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, ZN, VAL, MPD and ACN as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2BK7. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BO9 OCA].
+
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15738388 15738388]
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Aviles, F.X.]]
+
[[Category: Aviles FX]]
-
[[Category: Bonet, R.]]
+
[[Category: Bonet R]]
-
[[Category: Garcia-Castellanos, R.]]
+
[[Category: Garcia-Castellanos R]]
-
[[Category: Gomis-Rueth, F.X.]]
+
[[Category: Gomis-Rueth FX]]
-
[[Category: Pallares, I.]]
+
[[Category: Pallares I]]
-
[[Category: Vendrell, J.]]
+
[[Category: Vendrell J]]
-
[[Category: Ventura, S.]]
+
[[Category: Ventura S]]
-
[[Category: ACN]]
+
-
[[Category: MPD]]
+
-
[[Category: NAG]]
+
-
[[Category: VAL]]
+
-
[[Category: ZN]]
+
-
[[Category: endogenous protein inhibitor]]
+
-
[[Category: hydrolase]]
+
-
[[Category: latexin]]
+
-
[[Category: metallocarboxypeptidase]]
+
-
[[Category: metalloprotease carboxypeptidase]]
+
-
[[Category: x-ray crystal structure]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:26:07 2007''
+

Current revision

Human carboxypeptidase A4 in complex with human latexin.

PDB ID 2bo9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bo9"
Personal tools