4z88: Difference between revisions
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<StructureSection load='4z88' size='340' side='right'caption='[[4z88]], [[Resolution|resolution]] 2.09Å' scene=''> | <StructureSection load='4z88' size='340' side='right'caption='[[4z88]], [[Resolution|resolution]] 2.09Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4z88]] is a 24 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4z88]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z88 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4z88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z88 OCA], [https://pdbe.org/4z88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z88 RCSB], [https://www.ebi.ac.uk/pdbsum/4z88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z88 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/A0A0B4JDC9_DROME A0A0B4JDC9_DROME] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boehme | [[Category: Boehme MA]] | ||
[[Category: Driller | [[Category: Driller JH]] | ||
[[Category: Holton | [[Category: Holton N]] | ||
[[Category: Loll | [[Category: Loll B]] | ||
[[Category: Siebert | [[Category: Siebert M]] | ||
[[Category: Sigrist | [[Category: Sigrist SJ]] | ||
[[Category: Wahl | [[Category: Wahl MC]] | ||
Latest revision as of 13:58, 10 January 2024
SH3-II of Drosophila Rim-binding protein with Aplip1 peptideSH3-II of Drosophila Rim-binding protein with Aplip1 peptide
Structural highlights
FunctionPublication Abstract from PubMedSynaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co-accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 with submicromolar affinity. Pointmutating this PxxP motif provoked formation of ectopic AZ-like structures at axonal membranes. Direct interactions between AZ proteins and transport adaptors seem to provide complex avidity and shield synaptic interaction surfaces of pre-assembled scaffold protein transport complexes, thus, favouring physiological synaptic AZ assembly over premature assembly at axonal membranes. A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones.,Siebert M, Bohme MA, Driller JH, Babikir H, Mampell MM, Rey U, Ramesh N, Matkovic T, Holton N, Reddy-Alla S, Gottfert F, Kamin D, Quentin C, Klinedinst S, Andlauer TF, Hell SW, Collins CA, Wahl MC, Loll B, Sigrist SJ Elife. 2015 Aug 14;4. doi: 10.7554/eLife.06935. PMID:26274777[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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