5lk5: Difference between revisions

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'''Unreleased structure'''


The entry 5lk5 is ON HOLD
==Crystal structure of the globular domain of human calreticulin mutant D71K==
 
<StructureSection load='5lk5' size='340' side='right' caption='[[5lk5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
Authors: Gaboriaud, C., Cioci, G.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5lk5]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LK5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LK5 FirstGlance]. <br>
Description: Crystal structure of the globular domain of human calreticulin mutant D71K
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pow|3pow]]</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=5lk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lk5 OCA], [http://pdbe.org/5lk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lk5 RCSB], [http://www.ebi.ac.uk/pdbsum/5lk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lk5 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CALR_HUMAN CALR_HUMAN]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:7876246</ref> <ref>PMID:11149926</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cioci, G]]
[[Category: Gaboriaud, C]]
[[Category: Gaboriaud, C]]
[[Category: Cioci, G]]
[[Category: Calcium-binding protein]]

Revision as of 17:03, 10 September 2016

Crystal structure of the globular domain of human calreticulin mutant D71KCrystal structure of the globular domain of human calreticulin mutant D71K

Structural highlights

5lk5 is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CALR_HUMAN] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).[1] [2]

References

  1. ↑ Nauseef WM, McCormick SJ, Clark RA. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem. 1995 Mar 3;270(9):4741-7. PMID:7876246
  2. ↑ Holaska JM, Black BE, Love DC, Hanover JA, Leszyk J, Paschal BM. Calreticulin Is a receptor for nuclear export. J Cell Biol. 2001 Jan 8;152(1):127-40. PMID:11149926

5lk5, resolution 2.30Å

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