Cargando…
Structures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties
Calreticulin (CRT) is a multifaceted protein, initially discovered as an endoplasmic reticulum (ER) chaperone protein, that is essential in calcium metabolism. Various implications in cancer, early development and immunology have been discovered more recently for CRT, as well as its role as a domina...
Autores principales: | Moreau, Christophe, Cioci, Gianluca, Iannello, Marina, Laffly, Emmanuelle, Chouquet, Anne, Ferreira, Arturo, Thielens, Nicole M., Gaboriaud, Christine |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5094443/ https://www.ncbi.nlm.nih.gov/pubmed/27840680 http://dx.doi.org/10.1107/S2052252516012847 |
Ejemplares similares
-
Structural and Functional Characterization of a Single-Chain Form of the Recognition Domain of Complement Protein C1q
por: Moreau, Christophe, et al.
Publicado: (2016) -
X-Ray Structure of the Human Calreticulin Globular Domain Reveals a
Peptide-Binding Area and Suggests a Multi-Molecular Mechanism
por: Chouquet, Anne, et al.
Publicado: (2011) -
C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules
por: Jacquet, Mickaël, et al.
Publicado: (2018) -
The Interactions of Parasite Calreticulin With Initial Complement Components: Consequences in Immunity and Virulence
por: Ramírez-Toloza, Galia, et al.
Publicado: (2020) -
Molecular Basis of Complement C1q Collagen-Like Region Interaction with the Immunoglobulin-Like Receptor LAIR-1
por: Fouët, Guillaume, et al.
Publicado: (2021)