Structural characterization of human peptidyl-arginine deiminase type III by X-ray crystallography

被引：5

作者：

Rechiche, Othman ^{[1
]}

Lee, T. Verne ^{[2
]}

Lott, J. Shaun ^{[2
]}

机构：

[1] Penn State Univ, Dept Biochem & Mol Biol, Althouse Lab, Sci Dr, State Coll, PA 16801 USA

[2] Univ Auckland, Sch Biol Sci, 3a Symonds St, Auckland 1142, New Zealand

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2021年 / 77卷

关键词：

peptidyl-arginine deiminase; protein citrullination; calcium binding; hair follicles; post-translational modifications; KERATIN K1; PROTEINS; PURIFICATION; TRICHOHYALIN; SPECIFICITY; CITRULLINE; FEATURES; ENZYMES; GENES;

D O I：

10.1107/S2053230X21009195

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The Ca2+-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 angstrom. 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.

引用

页码：334 / 340

页数：7

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