9vvj: Difference between revisions

Latest revision as of 08:06, 25 March 2026

Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN

Structural highlights

9vvj is a 26 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.6Å
Ligands:	NAG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ERLN1_HUMAN Autosomal recessive spastic paraplegia type 62. The disease is caused by variants affecting the gene represented in this entry.

Function

ERLN1_HUMAN Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway (PubMed:37683630). Binds cholesterol and may promote ER retention of the SCAP-SREBF complex (PubMed:24217618).^[1] ^[2] ^[3] (Microbial infection) Required early in hepatitis C virus (HCV) infection to initiate RNA replication, and later in the infection to support infectious virus production.^[4]

References

↑ Pearce MM, Wormer DB, Wilkens S, Wojcikiewicz RJ. An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. J Biol Chem. 2009 Apr 17;284(16):10433-45. PMID:19240031 doi:10.1074/jbc.M809801200
↑ Huber MD, Vesely PW, Datta K, Gerace L. Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis. J Cell Biol. 2013 Nov 11;203(3):427-36. PMID:24217618 doi:10.1083/jcb.201305076
↑ Teo QW, Wong HH, Heunis T, Stancheva V, Hachim A, Lv H, Siu L, Ho J, Lan Y, Mok CKP, Ulferts R, Sanyal S. Usp25-Erlin1/2 activity limits cholesterol flux to restrict virus infection. Dev Cell. 2023 Nov 20;58(22):2495-2509.e6. PMID:37683630 doi:10.1016/j.devcel.2023.08.013
↑ Whitten-Bauer C, Chung J, Gómez-Moreno A, Gomollón-Zueco P, Huber MD, Gerace L, Garaigorta U. The Host Factor Erlin-1 is Required for Efficient Hepatitis C Virus Infection. Cells. 2019 Dec 2;8(12):1555. PMID:31810281 doi:10.3390/cells8121555

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Pearce MM, Wormer DB, Wilkens S, Wojcikiewicz RJ. An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. J Biol Chem. 2009 Apr 17;284(16):10433-45. PMID:19240031 doi:10.1074/jbc.M809801200

[2] Huber MD, Vesely PW, Datta K, Gerace L. Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis. J Cell Biol. 2013 Nov 11;203(3):427-36. PMID:24217618 doi:10.1083/jcb.201305076

[3] Teo QW, Wong HH, Heunis T, Stancheva V, Hachim A, Lv H, Siu L, Ho J, Lan Y, Mok CKP, Ulferts R, Sanyal S. Usp25-Erlin1/2 activity limits cholesterol flux to restrict virus infection. Dev Cell. 2023 Nov 20;58(22):2495-2509.e6. PMID:37683630 doi:10.1016/j.devcel.2023.08.013

[4] Whitten-Bauer C, Chung J, Gómez-Moreno A, Gomollón-Zueco P, Huber MD, Gerace L, Garaigorta U. The Host Factor Erlin-1 is Required for Efficient Hepatitis C Virus Infection. Cells. 2019 Dec 2;8(12):1555. PMID:31810281 doi:10.3390/cells8121555

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[2]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9vvj is ON HOLD  until Paper Publication
+==Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN==
+<StructureSection load='9vvj' size='340' side='right'caption='[[9vvj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9vvj]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VVJ FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9vvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vvj OCA], [https://pdbe.org/9vvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vvj RCSB], [https://www.ebi.ac.uk/pdbsum/9vvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vvj ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ERLN1_HUMAN ERLN1_HUMAN] Autosomal recessive spastic paraplegia type 62. The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/ERLN1_HUMAN ERLN1_HUMAN] Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway (PubMed:37683630). Binds cholesterol and may promote ER retention of the SCAP-SREBF complex (PubMed:24217618).<ref>PMID:19240031</ref> <ref>PMID:24217618</ref> <ref>PMID:37683630</ref>   (Microbial infection) Required early in hepatitis C virus (HCV) infection to initiate RNA replication, and later in the infection to support infectious virus production.<ref>PMID:31810281</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Gao N]]
+[[Category: Yan L]]

9vvj: Difference between revisions

Latest revision as of 08:06, 25 March 2026

Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN

Structural highlights

Disease

Function

References

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