5vnh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5vnh" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5vnh is ON HOLD
+
==Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal SV sorting motif==
 +
<StructureSection load='5vnh' size='340' side='right' caption='[[5vnh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5vnh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VNH FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vne|5vne]], [[5vnf|5vnf]], [[5vng|5vng]], [[5vni|5vni]], [[5vnj|5vnj]], [[5vnk|5vnk]], [[5vnl|5vnl]], [[5vnm|5vnm]], [[5vnn|5vnn]], [[5vno|5vno]]</td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEC23A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SEC24A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Sec22b, Sec22l1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5vnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vnh OCA], [http://pdbe.org/5vnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vnh RCSB], [http://www.ebi.ac.uk/pdbsum/5vnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vnh ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[[http://www.uniprot.org/uniprot/SC23A_HUMAN SC23A_HUMAN]] Defects in SEC23A are the cause of craniolenticulosutural dysplasia (CLSD) [MIM:[http://omim.org/entry/607812 607812]]; also known as cranio-lenticulo-sutural dysplasia. CLSD is an autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.<ref>PMID:16980979</ref>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/SC23A_HUMAN SC23A_HUMAN]] Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex. [[http://www.uniprot.org/uniprot/SC22B_MOUSE SC22B_MOUSE]] SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. [[http://www.uniprot.org/uniprot/SC24A_HUMAN SC24A_HUMAN]] Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Native cargo proteins exit the endoplasmic reticulum (ER) in COPII-coated vesicles, whereas resident and misfolded proteins are substantially excluded from vesicles by a retention mechanism that remains unresolved. We probed the ER retention process using the proteostasis regulator 4-phenylbutyrate (4-PBA), which we show targets COPII protein to reduce the stringency of retention. 4-PBA competes with p24 proteins to bind COPII. When p24 protein uptake is blocked, COPII vesicles package resident proteins and an ER-trapped mutant LDL receptor. We further show that 4-PBA triggers the secretion of a KDEL-tagged luminal resident, implying that a compromised retention mechanism causes saturation of the KDEL retrieval system. The results indicate that stringent ER retention requires the COPII coat machinery to actively sort biosynthetic cargo from diffusible misfolded and resident ER proteins.
-
Authors: Ma, W., Goldberg, J.
+
ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.,Ma W, Goldberg E, Goldberg J Elife. 2017 Jun 8;6. pii: e26624. doi: 10.7554/eLife.26624. PMID:28594326<ref>PMID:28594326</ref>
-
Description: Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal SV sorting motif
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Ma, W]]
+
<div class="pdbe-citations 5vnh" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Human]]
 +
[[Category: Lk3 transgenic mice]]
[[Category: Goldberg, J]]
[[Category: Goldberg, J]]
 +
[[Category: Ma, W]]
 +
[[Category: Copii]]
 +
[[Category: Er retention]]
 +
[[Category: P24]]
 +
[[Category: Protein transport]]
 +
[[Category: Trafficking]]

Revision as of 06:43, 16 November 2017

Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal SV sorting motif

5vnh, resolution 2.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5vnh"
Personal tools