6ce1: Difference between revisions
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The entry | ==Crystal structure of Peptidyl Arginine Deiminase Type III (PADI3)== | ||
<StructureSection load='6ce1' size='340' side='right'caption='[[6ce1]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ce1]] is a 1 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=6CE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CE1 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]] 2.8Å</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=6ce1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ce1 OCA], [https://pdbe.org/6ce1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ce1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ce1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ce1 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 == | |||
The Ca(2+)-dependent enzyme peptidyl-arginine deiminase type III (PAD3) catalyses the deimination of arginine residues to form citrulline residues in proteins such as keratin, filaggrin and trichohyalin. This is an important post-translation modification that is required for normal hair and skin formation in follicles and keratocytes. The structure of apo human PAD3 was determined by X-ray crystallography to a resolution of 2.8 A. The structure of PAD3 revealed a similar overall architecture to other PAD isoforms: the N-terminal and middle domains of PAD3 show sequence and structural variety, whereas the sequence and structure of the C-terminal catalytic domain is highly conserved. Structural analysis indicates that PAD3 is a dimer in solution, as is also the case for the PAD2 and PAD4 isoforms but not the PAD1 isoform. | |||
Structural characterization of human peptidyl-arginine deiminase type III by X-ray crystallography.,Rechiche O, Lee TV, Lott JS Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):334-340. doi: , 10.1107/S2053230X21009195. Epub 2021 Sep 21. PMID:34605437<ref>PMID:34605437</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ce1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Lee TV]] | |||
[[Category: Lott JS]] | |||
[[Category: Rechiche O]] | |||
Latest revision as of 15:02, 4 October 2023
Crystal structure of Peptidyl Arginine Deiminase Type III (PADI3)
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