View source for 7d5v


==Structure of the C646A mutant of peptidylarginine deiminase type III (PAD3)==
<StructureSection load='7d5v' size='340' side='right'caption='[[7d5v]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7d5v]] 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=7D5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D5V 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]] 2.102&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7d5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d5v OCA], [https://pdbe.org/7d5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d5v RCSB], [https://www.ebi.ac.uk/pdbsum/7d5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d5v ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/PADI3_HUMAN PADI3_HUMAN] Uncombable hair syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/PADI3_HUMAN PADI3_HUMAN] Catalyzes the deimination of arginine residues of proteins.<ref>PMID:27866708</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidylarginine deiminase type III (PAD3) is an isozyme belonging to the PAD enzyme family that converts arginine to citrulline residue(s) within proteins. PAD3 is expressed in most differentiated keratinocytes of the epidermis and hair follicles, while S100A3, trichohyalin, and filaggrin are its principal substrates. In this study, the X-ray crystal structures of PAD3 in six states, including its complex with the PAD inhibitor Cl-amidine, were determined. This structural analysis identified a large space around Gly374 in the PAD3-Ca(2+)-Cl-amidine complex, which may be used to develop novel PAD3-selective inhibitors. In addition, similarities between PAD3 and PAD4 were found based on the investigation of PAD4 reactivity with S100A3 in vitro. A comparison of the structures of PAD1, PAD2, PAD3, and PAD4 implied that the flexibility of the structures around the active site may lead to different substrate selectivity among these PAD isozymes.

Structures of human peptidylarginine deiminase type III provide insights into substrate recognition and inhibitor design.,Funabashi K, Sawata M, Nagai A, Akimoto M, Mashimo R, Takahara H, Kizawa K, Thompson PR, Ite K, Kitanishi K, Unno M Arch Biochem Biophys. 2021 May 7:108911. doi: 10.1016/j.abb.2021.108911. PMID:33971157<ref>PMID:33971157</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7d5v" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Akimoto M]]
[[Category: Mashimo R]]
[[Category: Unno M]]