1R64

The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor

1R64 の概要

• エントリーDOI: 10.2210/pdb1r64/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000420
• 分子名称: Kexin, Ac-Arg-Glu-Lys-boroArg peptide inhibitor, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: kex2, kexin, protease, protein convertase, prohormone processing, proprotein convertase, subtilisin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein: P13134
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108707.82

構造登録者

Holyoak, T.,Kettner, C.A.,Petsko, G.A.,Fuller, R.S.,Ringe, D. (登録日: 2003-10-14, 公開日: 2004-03-09, 最終更新日: 2024-10-16)

主引用文献

Holyoak, T.,Kettner, C.A.,Petsko, G.A.,Fuller, R.S.,Ringe, D.
Structural Basis for Differences in Substrate Selectivity in Kex2 and Furin Protein Convertases
Biochemistry, 43:2412-2421, 2004

PubMed Abstract: Kex2 is the yeast prototype of a large family of serine proteases that are highly specific for cleavage of their peptide substrates C-terminal to paired basic sites. This paper reports the 2.2 A resolution crystal structure of ssKex2 in complex with an Ac-Arg-Glu-Lys-Arg peptidyl boronic acid inhibitor (R = 19.7, R(free) = 23.4). By comparison of this structure with the structure of the mammalian homologue furin [Henrich, S., et al. (2003) Nat. Struct. Biol. 10, 520-526], we suggest a structural basis for the differences in substrate recognition at the P(2) and P(4) positions between Kex2 and furin and provide a structural rationale for the lack of P(6) recognition in Kex2. In addition, several monovalent cation binding sites are identified, and a mechanism of activation of Kex2 by potassium ion is proposed.

PubMed: 14992578
DOI: 10.1021/bi035849h

実験手法

X-RAY DIFFRACTION (2.2 Å)