Department of Biochemistry and Molecular Biology, The Pennsylvania State University, Althouse Laboratory, Science Drive, State College, PA 16801, USA.
School of Biological Sciences, The University of Auckland, 3a Symonds Street, Auckland 1142, New Zealand.
Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):334-340. doi: 10.1107/S2053230X21009195. Epub 2021 Sep 21.
The Ca-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 Å. 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.
钙依赖性酶肽基精氨酸脱亚氨酶 III（PAD3）催化精氨酸残基的脱亚氨作用，在角蛋白、板层素和毛透明蛋白等蛋白质中形成瓜氨酸残基。这是一种重要的翻译后修饰，对于毛囊和角质细胞中正常的毛发和皮肤形成是必需的。人源 PAD3 的apo 结构通过 X 射线晶体学解析到 2.8 Å 的分辨率。PAD3 的结构揭示了与其他 PAD 同工型相似的整体结构：PAD3 的 N 端和中间结构域显示出序列和结构的多样性，而 C 端催化结构域的序列和结构高度保守。结构分析表明，PAD3 在溶液中是二聚体，与 PAD2 和 PAD4 同工型的情况相同，但与 PAD1 同工型不同。
