3pos: Difference between revisions
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[[ | ==Crystal structure of the globular domain of human calreticulin== | ||
<StructureSection load='3pos' size='340' side='right' caption='[[3pos]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pos]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3POS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3POS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pow|3pow]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALR, CRTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pos RCSB], [http://www.ebi.ac.uk/pdbsum/3pos PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A 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. | |||
X-ray structure of the human calreticulin globular domain reveals a Peptide-binding area and suggests a multi-molecular mechanism.,Chouquet A, Paidassi H, Ling WL, Frachet P, Houen G, Arlaud GJ, Gaboriaud C PLoS One. 2011 Mar 15;6(3):e17886. PMID:21423620<ref>PMID:21423620</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Cytochrome P450|Cytochrome P450]] | *[[Cytochrome P450|Cytochrome P450]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arlaud, G J | [[Category: Arlaud, G J]] | ||
[[Category: Chouquet, A | [[Category: Chouquet, A]] | ||
[[Category: Frachet, P | [[Category: Frachet, P]] | ||
[[Category: Gaboriaud, C | [[Category: Gaboriaud, C]] | ||
[[Category: Houen, G | [[Category: Houen, G]] | ||
[[Category: Ling, W L | [[Category: Ling, W L]] | ||
[[Category: Paidassi, H | [[Category: Paidassi, H]] | ||
[[Category: Carbohydrate binding]] | [[Category: Carbohydrate binding]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
