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The Molecular Chaperone gp96/GRP94 Interacts with Toll-like Receptors and Integrins via Its C-terminal Hydrophobic Domain

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 i...

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Autores principales: Wu, Shuang, Hong, Feng, Gewirth, Daniel, Guo, Beichu, Liu, Bei, Li, Zihai
Formato: Artigo
Lenguaje:Inglês
Publicado: American Society for Biochemistry and Molecular Biology 2012
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC3307303/
https://ncbi.nlm.nih.gov/pubmed/22223641
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.309526
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