6ce1

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Peptidyl Arginine Deiminase Type III (PADI3)

Structural highlights

6ce1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PADI3_HUMAN Uncombable hair syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

PADI3_HUMAN Catalyzes the deimination of arginine residues of proteins.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ U Basmanav FB, Cau L, Tafazzoli A, Mechin MC, Wolf S, Romano MT, Valentin F, Wiegmann H, Huchenq A, Kandil R, Garcia Bartels N, Kilic A, George S, Ralser DJ, Bergner S, Ferguson DJP, Oprisoreanu AM, Wehner M, Thiele H, Altmuller J, Nurnberg P, Swan D, Houniet D, Buchner A, Weibel L, Wagner N, Grimalt R, Bygum A, Serre G, Blume-Peytavi U, Sprecher E, Schoch S, Oji V, Hamm H, Farrant P, Simon M, Betz RC. Mutations in Three Genes Encoding Proteins Involved in Hair Shaft Formation Cause Uncombable Hair Syndrome. Am J Hum Genet. 2016 Dec 1;99(6):1292-1304. doi: 10.1016/j.ajhg.2016.10.004. Epub, 2016 Nov 17. PMID:27866708 doi:http://dx.doi.org/10.1016/j.ajhg.2016.10.004
↑ Rechiche O, Lee TV, Lott JS. Structural characterization of human peptidyl-arginine deiminase type III by X-ray crystallography. Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):334-340. PMID:34605437 doi:10.1107/S2053230X21009195

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ce1"

Categories: Homo sapiens | Large Structures | Lee TV | Lott JS | Rechiche O

@@ Line 3: / Line 3: @@
 <StructureSection load='6ce1' size='340' side='right'caption='[[6ce1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ce1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
+<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PADI3, PAD3, PDI3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-arginine_deiminase Protein-arginine deiminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.15 3.5.3.15] </span></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.
+[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>
+[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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6ce1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Protein-arginine deiminase]]
+[[Category: Lee TV]]
-[[Category: Lee, T V]]
+[[Category: Lott JS]]
-[[Category: Lott, J S]]
+[[Category: Rechiche O]]
-[[Category: Rechiche, O]]
-[[Category: Citrullination calcium follicle hair skin]]
-[[Category: Hydrolase]]

6ce1

From Proteopedia

Current revision

Crystal structure of Peptidyl Arginine Deiminase Type III (PADI3)

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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