6n5y: Difference between revisions

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<StructureSection load='6n5y' size='340' side='right'caption='[[6n5y]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
<StructureSection load='6n5y' size='340' side='right'caption='[[6n5y]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6n5y]] is a 1 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=6N5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N5Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[6n5y]] is a 1 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=6N5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N5Y FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGF2R, MPRI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</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=6n5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n5y OCA], [http://pdbe.org/6n5y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n5y RCSB], [http://www.ebi.ac.uk/pdbsum/6n5y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n5y ProSAT]</span></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=6n5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n5y OCA], [https://pdbe.org/6n5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n5y RCSB], [https://www.ebi.ac.uk/pdbsum/6n5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n5y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SNX5_HUMAN SNX5_HUMAN]] May be involved in several stages of intracellular trafficking. Plays a role in macropinocytosis. Plays a role in the internalization of EGFR after EGF stimulation.<ref>PMID:18854019</ref> <ref>PMID:21048941</ref>
[https://www.uniprot.org/uniprot/SNX5_HUMAN SNX5_HUMAN] May be involved in several stages of intracellular trafficking. Plays a role in macropinocytosis. Plays a role in the internalization of EGFR after EGF stimulation.<ref>PMID:18854019</ref> <ref>PMID:21048941</ref> [https://www.uniprot.org/uniprot/MPRI_HUMAN MPRI_HUMAN] Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation, by binding DPP4.<ref>PMID:10900005</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein trafficking requires coat complexes that couple recognition of sorting motifs in transmembrane cargoes with biogenesis of transport carriers. The mechanisms of cargo transport through the endosomal network are poorly understood. Here, we identify a sorting motif for endosomal recycling of cargoes, including the cation-independent mannose-6-phosphate receptor and semaphorin 4C, by the membrane tubulating BAR domain-containing sorting nexins SNX5 and SNX6. Crystal structures establish that this motif folds into a beta-hairpin, which binds a site in the SNX5/SNX6 phox homology domains. Over sixty cargoes share this motif and require SNX5/SNX6 for their recycling. These include cargoes involved in neuronal migration and a Drosophila snx6 mutant displays defects in axonal guidance. These studies identify a sorting motif and provide molecular insight into an evolutionary conserved coat complex, the 'Endosomal SNX-BAR sorting complex for promoting exit 1' (ESCPE-1), which couples sorting motif recognition to the BAR-domain-mediated biogenesis of cargo-enriched tubulo-vesicular transport carriers.


Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins.,Simonetti B, Paul B, Chaudhari K, Weeratunga S, Steinberg F, Gorla M, Heesom KJ, Bashaw GJ, Collins BM, Cullen PJ Nat Cell Biol. 2019 Oct;21(10):1219-1233. doi: 10.1038/s41556-019-0393-3. Epub, 2019 Oct 1. PMID:31576058<ref>PMID:31576058</ref>
==See Also==
 
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6n5y" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Collins, B]]
[[Category: Collins B]]
[[Category: Paul, B]]
[[Category: Paul B]]
[[Category: Weeratunga, S]]
[[Category: Weeratunga S]]
[[Category: Endocytosis]]
[[Category: Endosome]]
[[Category: Snx]]
[[Category: Sorting nexin]]
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