Neutron crystallographic analysis of the nucleotide-binding domain of Hsp72 in complex with ADP

Neutron crystallographic analysis of the nucleotide-binding domain of Hsp72 in complex with ADP

The 70 kDa heat-shock proteins (Hsp70s) are ATP-dependent molecular chaperones that contain an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain. Hsp70s bind to misfolded/unfolded proteins and thereby prevent their aggregation. The ATP hydrolysis reaction in the NB...

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Bibliographic Details
Main Authors: Takeshi Yokoyama, Shiho Fujii, Andreas Ostermann, Tobias E. Schrader, Yuko Nabeshima, Mineyuki Mizuguchi
Format: Article
Language:English
Published: International Union of Crystallography 2022-09-01
Series:IUCrJ
Subjects:
neutron protein crystallography
heat-shock proteins
hsp72
hydrogen-bond networks
molecular chaperones
atpases
water clusters
Online Access:http://scripts.iucr.org/cgi-bin/paper?S2052252522006297

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http://scripts.iucr.org/cgi-bin/paper?S2052252522006297

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