[HTML][HTML] The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain
S Wu, F Hong, D Gewirth, B Guo, B Liu, Z Li - Journal of Biological …, 2012 - ASBMB
The structural basis for molecular chaperones to discern misfolded proteins has long been
an enigma. As the endoplasmic reticulum paralogue of the cytosolic HSP90, gp96 (GRP94,
HSP90b1) is an essential molecular chaperone for Toll-like receptors (TLRs) and integrins.
However, little is known about its client-binding domain (CBD). Herein, we provide genetic
and biochemical evidence to definitively demonstrate that a C-terminal loop structure,
formed by residues 652–678, is the critical region of CBD for both TLRs and integrins …
an enigma. As the endoplasmic reticulum paralogue of the cytosolic HSP90, gp96 (GRP94,
HSP90b1) is an essential molecular chaperone for Toll-like receptors (TLRs) and integrins.
However, little is known about its client-binding domain (CBD). Herein, we provide genetic
and biochemical evidence to definitively demonstrate that a C-terminal loop structure,
formed by residues 652–678, is the critical region of CBD for both TLRs and integrins …