Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1

Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1

Allosteric communication among domains in modular proteins consisting of flexibly linked domains with complimentary roles remains poorly understood. To understand how complementary domains communicate, we have studied human Pin1, a representative modular protein with two domains mutually tethered by...

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Bibliographic Details
Main Authors: Jing Wang, Ryosuke Kawasaki, Jun-ichi Uewaki, Arif U. R. Rashid, Naoya Tochio, Shin-ichi Tate
Format: Article
Language:English
Published: MDPI AG 2017-06-01
Series:Molecules
Subjects:
dynamic allostery
human Pin1
structure dynamics
spin relaxation
hydrogen bond
H/D exchange
NMR
Online Access:http://www.mdpi.com/1420-3049/22/6/992

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http://www.mdpi.com/1420-3049/22/6/992

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