5elq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5elq' size='340' side='right' caption='[[5elq]], [[Resolution|resolution]] 1.10Å' scene=''> | <StructureSection load='5elq' size='340' side='right' caption='[[5elq]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5elq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ELQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ELQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[5elq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ELQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ELQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z8j|4z8j]], [[5em9|5em9]], [[5ema|5ema]], [[5emb|5emb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z8j|4z8j]], [[5em9|5em9]], [[5ema|5ema]], [[5emb|5emb]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Snx27, Mrt1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=5elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5elq OCA], [http://pdbe.org/5elq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5elq RCSB], [http://www.ebi.ac.uk/pdbsum/5elq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5elq ProSAT]</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=5elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5elq OCA], [http://pdbe.org/5elq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5elq RCSB], [http://www.ebi.ac.uk/pdbsum/5elq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5elq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| Line 23: | Line 24: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | |||
[[Category: Clairfeuille, T]] | [[Category: Clairfeuille, T]] | ||
[[Category: Collins, B M]] | [[Category: Collins, B M]] | ||
Revision as of 15:38, 6 November 2017
Crystal structure of the SNX27 PDZ domain bound to the C-terminal DGKzeta PDZ binding motifCrystal structure of the SNX27 PDZ domain bound to the C-terminal DGKzeta PDZ binding motif
Structural highlights
Function[SNX27_RAT] Involved in endocytic trafficking (By similarity). In T lymphocytes, participates in endocytic recycling pathway. Recruits PSCDBP and HT4R to early endosomes (By similarity). Publication Abstract from PubMedRecycling of internalized receptors from endosomal compartments is essential for the receptors' cell-surface homeostasis. Sorting nexin 27 (SNX27) cooperates with the retromer complex in the recycling of proteins containing type I PSD95-Dlg-ZO1 (PDZ)-binding motifs. Here we define specific acidic amino acid sequences upstream of the PDZ-binding motif required for high-affinity engagement of the human SNX27 PDZ domain. However, a subset of SNX27 ligands, such as the beta2 adrenergic receptor and N-methyl-D-aspartate (NMDA) receptor, lack these sequence determinants. Instead, we identified conserved sites of phosphorylation that substitute for acidic residues and dramatically enhance SNX27 interactions. This newly identified mechanism suggests a likely regulatory switch for PDZ interaction and protein transport by the SNX27-retromer complex. Defining this SNX27 binding code allowed us to classify more than 400 potential SNX27 ligands with broad functional implications in signal transduction, neuronal plasticity and metabolite transport. A molecular code for endosomal recycling of phosphorylated cargos by the SNX27-retromer complex.,Clairfeuille T, Mas C, Chan AS, Yang Z, Tello-Lafoz M, Chandra M, Widagdo J, Kerr MC, Paul B, Merida I, Teasdale RD, Pavlos NJ, Anggono V, Collins BM Nat Struct Mol Biol. 2016 Sep 5. doi: 10.1038/nsmb.3290. PMID:27595347[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||