Monomeric Form of Peptidylarginine Deiminase Type I Revealed by X-ray Crystallography and Small-Angle X-ray Scattering
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- 作者：Shinya Saijo1 ; &dagger ; ; Anna Nagai2 ; 3 ; &dagger ; ; Saya Kinjo4 ; Ryutaro Mashimo2 ; 3 ; Megumi Akimoto2 ; 3 ; Kenji Kizawa5 ; Toshiki Yabe-Wada6 ; Nobutaka Shimizu1 ; Hidenari Takahara3 ; 4 ; Masaki Unno2 ; 3 ; masaki.unno.19@vc.ibaraki.ac.jp" class="auth_mail" title="E-mail the corresponding author
- 关键词：PAD ; peptidylarginine deiminase ; SAXS ; small-angle X-ray scattering ; NCS ; non-crystallographic symmetry ; IgG ; immunoglobulin ; CD ; catalytic domain ; PDB ; protein data bank ; WT ; wild-type ; BAA ; benzoyl-L-arginine amide ; PPAD ; Porphyromonas gingivalis PAD ; Rg ; radius of gyration ; Mr ; molecular mass ; Dmax ; maximum molecular dimension ; B-factor ; temperature factor ; BAEE ; benzoyl-L-arginine ethyl ester ; ITC ; isothermal titration calorimetry
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：31 July 2016
- 年：2016
- 卷：428
- 期：15
- 页码：3058-3073
- 全文大小：2398 K
文摘
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Both the solution structure and the crystal structure of peptidylarginine deiminase type 1 (PAD1) were determined for the first time.
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PAD1 has an elongated N-terminal tail structure, which is not found in PAD2 and PAD4.
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PAD1 exists as the monomer, whereas PAD2, PAD3, and PAD4 exist as the homodimer.
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The monomeric form of PAD1 is advantageous to its broader substrate specificity.