6NVB

Crystal structure of the inhibitor-free form of the serine protease kallikrein-4

6NVB の概要

• エントリーDOI: 10.2210/pdb6nvb/pdb
• 分子名称: Kallikrein-4, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: protease, klk4, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96797.05

構造登録者

Riley, B.T.,Buckle, A.M.,McGowan, S. (登録日: 2019-02-04, 公開日: 2019-07-17, 最終更新日: 2024-11-20)

主引用文献

Riley, B.T.,Hoke, D.E.,McGowan, S.,Buckle, A.M.
Crystal structure of the inhibitor-free form of the serine protease kallikrein-4.
Acta Crystallogr.,Sect.F, 75:543-546, 2019

PubMed Abstract: Kallikrein 4 (KLK4) is a serine protease that is predominantly expressed in the prostate and is overexpressed in prostate cancer. As such, it has gained attention as an attractive target for prostate cancer therapeutics. Currently, only liganded structures of KLK4 exist in the Protein Data Bank. Until now, inferences about the subtle structural changes in KLK4 upon ligand binding have been made by comparison to other liganded forms, rather than to an apo form. In this study, an inhibitor-free form of KLK4 was crystallized. The crystals obtained belonged to space group P1, contained four molecules in the asymmetric unit and diffracted to 1.64 Å resolution. Interestingly, a nonstandard rotamer of the specificity-determining residue Asp189 was observed in all chains. This model will provide a useful unliganded structure for the future structure-guided design of KLK4 inhibitors.

PubMed: 31397325
DOI: 10.1107/S2053230X19009610

実験手法

X-RAY DIFFRACTION (1.636 Å)