Structural insights into complexes of glucose-regulated Protein94 (Grp94) with human immunoglobulin G. relevance for Grp94-IgG complexes that form in vivo in pathological conditions.

Structural insights into complexes of glucose-regulated Protein94 (Grp94) with human immunoglobulin G. relevance for Grp94-IgG complexes that form in vivo in pathological conditions.

While the mechanism by which Grp94 displays its chaperone function with client peptides in the cell has been elucidated extensively, much less is known about the nature and properties of how Grp94 can engage binding to proteins once it is exposed on the cell surface or liberated in the extra-cellula...

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Bibliographic Details
Main Authors: Andrea Pagetta, Elisa Tramentozzi, Elena Tibaldi, Laura Cendron, Giuseppe Zanotti, Anna Maria Brunati, Maurizio Vitadello, Luisa Gorza, Paola Finotti
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3904872?pdf=render

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http://europepmc.org/articles/PMC3904872?pdf=render

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