7oit
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of AP2 Mu2 in complex with FCHO2 WxxPhi motif (P3221 crystal form)== | |
- | + | <StructureSection load='7oit' size='340' side='right'caption='[[7oit]], [[Resolution|resolution]] 1.65Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[7oit]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OIT FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | |
- | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7oit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oit OCA], [https://pdbe.org/7oit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oit RCSB], [https://www.ebi.ac.uk/pdbsum/7oit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oit ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A0A140TAH5_RAT A0A140TAH5_RAT] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules.[PIRNR:PIRNR005992] | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Rattus norvegicus]] | ||
+ | [[Category: Evans PR]] | ||
+ | [[Category: Kelly BT]] | ||
+ | [[Category: Owen DJ]] | ||
+ | [[Category: Zaccai NR]] |
Current revision
Crystal structure of AP2 Mu2 in complex with FCHO2 WxxPhi motif (P3221 crystal form)
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