6ce1

Crystal structure of Peptidyl Arginine Deiminase Type III (PADI3)

spinqualitylabelsall models 6ce1, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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