5v90: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5v90 is ~~ON HOLD~~ ~~until Paper Publication~~

==Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[5v90]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V90 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V90 FirstGlance].

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[5v8z|5v8z]]</td></tr>

<tr id='gene'><td class="sblockLbl">[[Gene|Gene:]]</td><td class="sblockDat">ERP29, C12orf8, ERP28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CALR, CRTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5v90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v90 OCA], [http://pdbe.org/5v90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v90 RCSB], [http://www.ebi.ac.uk/pdbsum/5v90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v90 ProSAT]</td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/ERP29_HUMAN ERP29_HUMAN]] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. [[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 ==

__TOC__

</StructureSection>

[[Category: Human]]

[[Category: Gehring, K]]

[[Category: Kozlov, G]]

[[Category: Munoz-Escobar, J]]

[[Category: Chaperone]]

[[Category: Protein binding]]

[[Category: Protein folding]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5v90 is ON HOLD  until Paper Publication
+==Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin==
+<StructureSection load='5v90' size='340' side='right' caption='[[5v90]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5v90]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V90 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v8z|5v8z]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERP29, C12orf8, ERP28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CALR, CRTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5v90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v90 OCA], [http://pdbe.org/5v90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v90 RCSB], [http://www.ebi.ac.uk/pdbsum/5v90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v90 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ERP29_HUMAN ERP29_HUMAN]] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. [[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: Human]]
+[[Category: Gehring, K]]
+[[Category: Kozlov, G]]
+[[Category: Munoz-Escobar, J]]
+[[Category: Chaperone]]
+[[Category: Protein binding]]
+[[Category: Protein folding]]