Calreticulin: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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 <StructureSection load='6eny' size='340' side='right' caption='Human calreticulin (gold) complex with β-microglobulin (green), tapasin (pink),  protein disulfide-isomerase (yellow) MHC class I antigen (cyan) (PDB code [[6eny]]) ' scene=''>
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 == Structural highlights ==
-CALR structure consists of 3 domains: N-terminal globular domain which has chaperone function; P-domain which is proline-rich, binds Ca+2 with high affinity and possesses a lectin-like chaperone function; C-terminal domain containing an ER retention signal.
+<scene name='77/776393/Cv/1'>CALR structure consists of 3 domains</scene>: N-terminal globular domain which has chaperone function; P-domain which is proline-rich, binds Ca+2 with high affinity and possesses a lectin-like chaperone function; C-terminal domain containing an ER retention signal.
-</StructureSection>
 == 3D Structures of calreticulin ==
+[[Calreticulin 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+</StructureSection>
-[[1hhn]], [[1k91]], [[1k9c]] – CALR P domain 189-288 – rat - NMR <br />
-[[6eny]] – hCALR + β-microglobulin + tapasin + protein disulfide-isomerase + MHC class I antigen – human <br />
-[[5v90]] – hCALR P domain 238-273 + ERP29 <br />
-[[3o0v]], [[3o0w]], [[3o0x]], [[3rg0]] – CALR lectin domain 18-206 301-368 (mutant) – mouse <br />
-[[3pos]], [[3pow]] – hCALR lectin domain 18-206 301-368 <br />
-[[5lk5]] – hCALR lectin domain 18-206 301-368 (mutant) <br />
-[[5hca]], [[5hcb]] – CALR lectin domain 18-206 301-368 + glucose – ''Entamoeba histolytica'' <br />
 == References ==
 <references/>
 [[Category:Topic Page]]