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| | ==Crystal structure of Rat Mint2 PPC== | | ==Crystal structure of Rat Mint2 PPC== |
| - | <StructureSection load='3suz' size='340' side='right' caption='[[3suz]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='3suz' size='340' side='right'caption='[[3suz]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3suz]] is a 1 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=3SUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SUZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3suz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SUZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sv1|3sv1]]</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]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mint2 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3suz OCA], [https://pdbe.org/3suz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3suz RCSB], [https://www.ebi.ac.uk/pdbsum/3suz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3suz 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=3suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3suz OCA], [http://pdbe.org/3suz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3suz RCSB], [http://www.ebi.ac.uk/pdbsum/3suz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3suz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/APBA2_RAT APBA2_RAT]] Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP. | + | [https://www.uniprot.org/uniprot/APBA2_RAT APBA2_RAT] Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP. |
| | <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: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Long, J]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Shen, Y]] | + | [[Category: Long J]] |
| - | [[Category: Xie, X]] | + | [[Category: Shen Y]] |
| - | [[Category: Yan, X]] | + | [[Category: Xie X]] |
| - | [[Category: App binding]]
| + | [[Category: Yan X]] |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
APBA2_RAT Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.
Publication Abstract from PubMed
Amyloid-beta protein precursor (APP) plays a crucial role in the pathogenesis of Alzheimer's disease (AD). Knock-out and transgenic mouse studies of the adaptor protein Mint2 have revealed that it is a major player in regulating APP metabolism physiologically through the binding of its PTB domain to the intracellular domain of APP. However, the molecular mechanism of APP dynamically binding to Mint2 remains elusive. Here, we report the structures of APP peptide-free and APP peptide-bound C-terminal Mint2 mutants at resolutions of 2.7 and 3.3 A, respectively. Our structures reveal that APP peptide-free Mint2 exists in a closed state in which the ARM domain blocks the peptide binding groove of the PTB domain. In sharp contrast, APP peptide-bound Mint2 exists in an open state in which the ARM domain drastically swings away from the bound peptide. Mutants that control the open-closed motion of Mint2 dynamically regulated APP metabolism both in vitro and in vivo. Our results uncover a novel open-closed mechanism of the PTB domain dynamically binding to its peptide substrate. Moreover, such a conformational switch may represent a general regulation mode of APP family members by Mint proteins, providing useful information for the treatment of AD.
Open-closed motion of Mint2 regulates APP metabolism.,Xie X, Yan X, Wang Z, Zhou H, Diao W, Zhou W, Long J, Shen Y J Mol Cell Biol. 2012 Jun 21. PMID:22730553[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xie X, Yan X, Wang Z, Zhou H, Diao W, Zhou W, Long J, Shen Y. Open-closed motion of Mint2 regulates APP metabolism. J Mol Cell Biol. 2012 Jun 21. PMID:22730553 doi:10.1093/jmcb/mjs033
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