6GID

High resolution crystal structure of substrate-free human neprilysin

6GID の概要

• エントリーDOI: 10.2210/pdb6gid/pdb
• 分子名称: Neprilysin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (9 entities in total)
• 機能のキーワード: substrate-free, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81477.59

構造登録者

Moss, S.,Subramanian, V.,Acharya, K.R. (登録日: 2018-05-10, 公開日: 2018-06-27, 最終更新日: 2024-10-23)

主引用文献

Moss, S.,Subramanian, V.,Acharya, K.R.
High resolution crystal structure of substrate-free human neprilysin.
J. Struct. Biol., 204:19-25, 2018

PubMed Abstract: Neprilysin is a transmembrane M13 zinc metalloprotease responsible for the degradation of several biologically active peptides including insulin, enkephalin, substance P, bradykinin, endothelin-1, neurotensin and amyloid-β. The protein has received attention for its role in modulating blood pressure responses with its inhibition producing an antihypertensive response. To date, several inhibitor bound crystal structures of the human neprilysin extracellular domain have been determined, but, a structure free of bound inhibitor or substrate has yet to be reported. Here, we report the first crystal structure free of substrate or inhibitor for the extracellular catalytic domain of human neprilysin at 1.9 Å resolution. This structure will provide a reference point for comparisons to future inhibitor or substrate bound structures. The neprilysin structure also reveals that a closed protein conformation can be adopted in protein crystals absent of bound substrate or inhibitor.

PubMed: 29906506
DOI: 10.1016/j.jsb.2018.06.004

実験手法

X-RAY DIFFRACTION (1.9 Å)