2r2j

From Proteopedia

(Difference between revisions)

Revision as of 19:27, 10 September 2015

crystal structure of human ERp44

Structural highlights

2r2j is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	TXNDC4, ERP44, KIAA0573 (Homo sapiens)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ERP44_HUMAN] Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif. Here, we present its crystal structure at a resolution of 2.6 A. Three thioredoxin domains-a, b and b'-are arranged in a clover-like structure. A flexible carboxy-terminal tail turns back to the b' and a domains, shielding a hydrophobic pocket in domain b' and a hydrophobic patch around the CRFS motif in domain a. Mutational and functional studies indicate that the C-terminal tail gates the CRFS area and the adjacent hydrophobic pocket, dynamically regulating protein quality control.

Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail.,Wang L, Wang L, Vavassori S, Li S, Ke H, Anelli T, Degano M, Ronzoni R, Sitia R, Sun F, Wang CC EMBO Rep. 2008 Jul;9(7):642-7. Epub 2008 Jun 13. PMID:18552768^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 2002 Feb 15;21(4):835-44. PMID:11847130 doi:http://dx.doi.org/10.1093/emboj/21.4.835
↑ Anelli T, Alessio M, Bachi A, Bergamelli L, Bertoli G, Camerini S, Mezghrani A, Ruffato E, Simmen T, Sitia R. Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J. 2003 Oct 1;22(19):5015-22. PMID:14517240 doi:http://dx.doi.org/10.1093/emboj/cdg491
↑ Wang L, Wang L, Vavassori S, Li S, Ke H, Anelli T, Degano M, Ronzoni R, Sitia R, Sun F, Wang CC. Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail. EMBO Rep. 2008 Jul;9(7):642-7. Epub 2008 Jun 13. PMID:18552768 doi:10.1038/embor.2008.88

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2r2j"

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TXNDC4, ERP44, KIAA0573 ([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=2r2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r2j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r2j RCSB], [http://www.ebi.ac.uk/pdbsum/2r2j PDBsum]</span></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=2r2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r2j OCA], [http://pdbe.org/2r2j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r2j RCSB], [http://www.ebi.ac.uk/pdbsum/2r2j PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TXND4_HUMAN TXND4_HUMAN]] Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum.<ref>PMID:11847130</ref> <ref>PMID:14517240</ref>
+[[http://www.uniprot.org/uniprot/ERP44_HUMAN ERP44_HUMAN]] Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum.<ref>PMID:11847130</ref> <ref>PMID:14517240</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2r2j" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2r2j

From Proteopedia

Revision as of 19:27, 10 September 2015

crystal structure of human ERp44

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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