Crystal structure of plasma kallikrein reveals the unusual flexibility of the S1 pocket triggered by Glu217 - Details

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Abstract：

Serine　proteases　play　important　roles　in　numerous　physiological　and　pathophysiological　processes.　Moreover,　serine　proteases　are　classical　subjects　for　studies　of　catalytic　and　inhibitory　mechanisms　of　enzymes.　Here,　we　determined　the　crystal　structures　of　a　serine　protease,　murine　plasma　kallikrein　(mPK),　and　its　complex　with　a　peptidic　inhibitor.　Although　mPK　in　the　complex　adopts　a　canonical　protease　structure,　the　apo-mPK　exhibits　a　previously　unobserved　structural　feature:　the　entrance　of　the　intact　S1　pocket　is　blocked　by　Glu217.　In　addition,　molecular　dynamics　simulations　and　functional　assays　support　the　flexibility　of　Glu217　and　suggest　that　this　flexibility　plays　a　role　in　regulating　the　activity　of　serine　proteases.　Enzymes:　EC:　3.4.21.34.　©　2018　Federation　of　European　Biochemical　Societies

Keyword：

flexibility; molecular dynamics; plasma kallikrein; serine proteases; X-ray crystallography

Community：

[ 1 ] [Xu, M.]College of Chemistry, Fuzhou University, China
[ 2 ] [Xu, M.]Fujian Institute of Research on the Structure of Matter, State Key Laboratory of Structural Chemistry, Chinese Academy of Sciences, Fuzhou, China
[ 3 ] [Chen, Y.]College of Chemistry, Fuzhou University, China
[ 4 ] [Xu, P.]Fujian Institute of Research on the Structure of Matter, State Key Laboratory of Structural Chemistry, Chinese Academy of Sciences, Fuzhou, China
[ 5 ] [Andreasen, P.A.]Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark
[ 6 ] [Jiang, L.]College of Chemistry, Fuzhou University, China
[ 7 ] [Li, J.]College of Chemistry, Fuzhou University, China
[ 8 ] [Huang, M.]College of Chemistry, Fuzhou University, China
[ 9 ] [Huang, M.]Fujian Institute of Research on the Structure of Matter, State Key Laboratory of Structural Chemistry, Chinese Academy of Sciences, Fuzhou, China

Reprint 's Address：

[Jiang, L.]College of Chemistry, Fuzhou UniversityChina

Email：

jianglg@fzu.edu.cn

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Source ：

FEBS Letters

ISSN： 0014-5793

Year： 2018

Issue： 15

Volume： 592

Page： 2658-2667

2 . 6 7 5

JCR@2018

3 . 0 0 0

JCR@2023

ESI HC Threshold：212

JCR Journal Grade：2

CAS Journal Grade：2

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ESI Highly Cited Papers on the List： 0 Unfold All

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