X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.

In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55 Å resolution. Interactions of the flexible N-term...

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Autores principales:	Anne Chouquet, Helena Païdassi, Wai Li Ling, Philippe Frachet, Gunnar Houen, Gérard J Arlaud, Christine Gaboriaud
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/eaade0fab6c445af9f24313a60756608
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spelling	oai:doaj.org-article:eaade0fab6c445af9f24313a607566082021-11-18T06:57:16ZX-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.1932-620310.1371/journal.pone.0017886https://doaj.org/article/eaade0fab6c445af9f24313a607566082011-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21423620/?tool=EBIhttps://doaj.org/toc/1932-6203In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55 Å resolution. Interactions of the flexible N-terminal extension with the edge of the lectin site are consistently observed, revealing a hitherto unidentified peptide-binding site. A calreticulin molecular zipper, observed in all crystal lattices, could further extend this site by creating a binding cavity lined by hydrophobic residues. These data thus provide a first structural insight into the lectin-independent binding properties of calreticulin and suggest new working hypotheses, including that of a multi-molecular mechanism.Anne ChouquetHelena PaïdassiWai Li LingPhilippe FrachetGunnar HouenGérard J ArlaudChristine GaboriaudPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 3, p e17886 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anne Chouquet Helena Païdassi Wai Li Ling Philippe Frachet Gunnar Houen Gérard J Arlaud Christine Gaboriaud X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
description	In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55 Å resolution. Interactions of the flexible N-terminal extension with the edge of the lectin site are consistently observed, revealing a hitherto unidentified peptide-binding site. A calreticulin molecular zipper, observed in all crystal lattices, could further extend this site by creating a binding cavity lined by hydrophobic residues. These data thus provide a first structural insight into the lectin-independent binding properties of calreticulin and suggest new working hypotheses, including that of a multi-molecular mechanism.
format	article
author	Anne Chouquet Helena Païdassi Wai Li Ling Philippe Frachet Gunnar Houen Gérard J Arlaud Christine Gaboriaud
author_facet	Anne Chouquet Helena Païdassi Wai Li Ling Philippe Frachet Gunnar Houen Gérard J Arlaud Christine Gaboriaud
author_sort	Anne Chouquet
title	X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
title_short	X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
title_full	X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
title_fullStr	X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
title_full_unstemmed	X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
title_sort	x-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/eaade0fab6c445af9f24313a60756608
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X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.

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