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[[Image:1qmu.gif|left|200px]]<br />
<applet load="1qmu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qmu, resolution 2.70&Aring;" />
'''DUCK CARBOXYPEPTIDASE D DOMAIN II'''<br />


==Overview==
==Duck carboxypeptidase D domain II==
The crystal structure of domain II of duck carboxypeptidase D, a, prohormone/propeptide processing enzyme integrated in a three repeat, tandem in the natural system, has been solved, constituting a prototype, for members of the regulatory metallocarboxypeptidase subfamily. It, displays a 300 residue N-terminal alpha/beta-hydrolase subdomain with, overall topological similarity to and general coincidence of the key, catalytic residues with the archetypal pancreatic carboxypeptidase A., However, numerous significant insertions/deletions in segments forming the, funnel-like access to the active site explain differences in specificity, towards larger protein substrates or inhibitors. This alpha/beta-hydrolase, subdomain is followed by a C-terminal 80 residue beta-sandwich subdomain, unique for these regulatory metalloenzymes and topologically related to, transthyretin and sugar-binding proteins. The structure described here, establishes the fundamentals for a better understanding of the mechanism, ruling events such as prohormone processing and will enable modelling of, regulatory carboxypeptidases as well as a more rational design of, inhibitors of carboxypeptidase D.
<StructureSection load='1qmu' size='340' side='right'caption='[[1qmu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qmu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lophonetta_specularioides Lophonetta specularioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QMU 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmu OCA], [https://pdbe.org/1qmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qmu RCSB], [https://www.ebi.ac.uk/pdbsum/1qmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qmu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBPD_LOPSP CBPD_LOPSP]
== 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/qm/1qmu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1qmu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a prototype for members of the regulatory metallocarboxypeptidase subfamily. It displays a 300 residue N-terminal alpha/beta-hydrolase subdomain with overall topological similarity to and general coincidence of the key catalytic residues with the archetypal pancreatic carboxypeptidase A. However, numerous significant insertions/deletions in segments forming the funnel-like access to the active site explain differences in specificity towards larger protein substrates or inhibitors. This alpha/beta-hydrolase subdomain is followed by a C-terminal 80 residue beta-sandwich subdomain, unique for these regulatory metalloenzymes and topologically related to transthyretin and sugar-binding proteins. The structure described here establishes the fundamentals for a better understanding of the mechanism ruling events such as prohormone processing and will enable modelling of regulatory carboxypeptidases as well as a more rational design of inhibitors of carboxypeptidase D.


==About this Structure==
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily.,Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M EMBO J. 1999 Nov 1;18(21):5817-26. PMID:10545093<ref>PMID:10545093</ref>
1QMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anas_specularioides Anas specularioides] with SO4 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: ZN. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QMU OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily., Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M, EMBO J. 1999 Nov 1;18(21):5817-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10545093 10545093]
</div>
[[Category: Anas specularioides]]
<div class="pdbe-citations 1qmu" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Aviles, F.X.]]
[[Category: Coll, M.]]
[[Category: Fricker, L.D.]]
[[Category: Gomis-Rueth, F.X.]]
[[Category: Vendrell, J.]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: carboxypeptidase]]
[[Category: hydrolase]]
[[Category: zinc-dependent protease]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:30:00 2007''
==See Also==
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lophonetta specularioides]]
[[Category: Aviles FX]]
[[Category: Coll M]]
[[Category: Fricker LD]]
[[Category: Gomis-Rueth FX]]
[[Category: Vendrell J]]
Retrieved from "https://proteopedia.org/1qmu"