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< | ==Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4== | ||
<StructureSection load='4a94' size='340' side='right'caption='[[4a94]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a94]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Nerita_versicolor Nerita versicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A94 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]] 1.7Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=4a94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a94 OCA], [https://pdbe.org/4a94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a94 RCSB], [https://www.ebi.ac.uk/pdbsum/4a94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a94 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NvCI is a novel exogenous proteinaceous inhibitor of metallo-carboxypeptidases from the marine snail Nerita versicolor. The complex between human carboxypeptidase 4 (hCPA4) and NvCI has been crystallized and determined at 1.7 A resolution. The NvCI structure defines a distinctive protein fold basically composed by a two-stranded antiparallel beta-sheet connected by three loops, the inhibitory C-terminal tail and stabilized by three disulphide bridges. NvCI is a tight-binding inhibitor that interacts with the active site of the enzyme in a substrate-like manner. NvCI displays an extended and novel interface with hCPA4, responsible of inhibitory constant values in the picomolar range for some members of the M14A subfamily of carboxypeptidases. This makes NvCI the strongest inhibitor reported so far for this family. The structural homology displayed by the C-terminal tails of different carboxypeptidase inhibitors represents a relevant example of convergent evolution. | |||
Crystal structure of a novel metallo-carboxypeptidase inhibitor from the marine mollusk Nerita versicolor in complex with human carboxypeptidase A4.,Covaleda G, Alonso Del Rivero M, Chavez MA, Aviles FX, Reverter D J Biol Chem. 2012 Jan 31. PMID:22294694<ref>PMID:22294694</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a94" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | |||
[[Category: Nerita versicolor]] | [[Category: Nerita versicolor]] | ||
[[Category: Alonso | [[Category: Alonso M]] | ||
[[Category: Aviles | [[Category: Aviles FX]] | ||
[[Category: Chavez | [[Category: Chavez MA]] | ||
[[Category: Covaleda | [[Category: Covaleda G]] | ||
[[Category: Reverter | [[Category: Reverter D]] | ||
Latest revision as of 05:40, 21 November 2024
Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4
Structural highlights
Publication Abstract from PubMedNvCI is a novel exogenous proteinaceous inhibitor of metallo-carboxypeptidases from the marine snail Nerita versicolor. The complex between human carboxypeptidase 4 (hCPA4) and NvCI has been crystallized and determined at 1.7 A resolution. The NvCI structure defines a distinctive protein fold basically composed by a two-stranded antiparallel beta-sheet connected by three loops, the inhibitory C-terminal tail and stabilized by three disulphide bridges. NvCI is a tight-binding inhibitor that interacts with the active site of the enzyme in a substrate-like manner. NvCI displays an extended and novel interface with hCPA4, responsible of inhibitory constant values in the picomolar range for some members of the M14A subfamily of carboxypeptidases. This makes NvCI the strongest inhibitor reported so far for this family. The structural homology displayed by the C-terminal tails of different carboxypeptidase inhibitors represents a relevant example of convergent evolution. Crystal structure of a novel metallo-carboxypeptidase inhibitor from the marine mollusk Nerita versicolor in complex with human carboxypeptidase A4.,Covaleda G, Alonso Del Rivero M, Chavez MA, Aviles FX, Reverter D J Biol Chem. 2012 Jan 31. PMID:22294694[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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