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| | <StructureSection load='5k7b' size='340' side='right'caption='[[5k7b]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5k7b' size='340' side='right'caption='[[5k7b]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k7b]] is a 4 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=5K7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K7B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k7b]] is a 4 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=5K7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K7B FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BECN2, BECN1L1, BECN1P1 ([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]] 2.3Å</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=5k7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7b OCA], [http://pdbe.org/5k7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k7b RCSB], [http://www.ebi.ac.uk/pdbsum/5k7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7b 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=5k7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7b OCA], [https://pdbe.org/5k7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k7b RCSB], [https://www.ebi.ac.uk/pdbsum/5k7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BECN2_HUMAN BECN2_HUMAN]] Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1.<ref>PMID:23954414</ref> | + | [https://www.uniprot.org/uniprot/BECN2_HUMAN BECN2_HUMAN] Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1.<ref>PMID:23954414</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
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| - | ATG14 binding to BECN/Beclin homologs is essential for autophagy, a critical catabolic homeostasis pathway. Here we show that the alpha-helical, coiled-coil domain (CCD) of BECN2, a recently identified mammalian BECN1 paralog, forms an anti-parallel, curved homodimer with seven pairs of non-ideal packing interactions, while the BECN2 CCD and ATG14 CCD form a parallel, curved heterodimer stabilized by multiple, conserved polar interactions. Compared to BECN1, the BECN2 CCD forms a weaker homodimer, but binds more tightly to the ATG14 CCD. Mutation of non-ideal BECN2 interface residues to more ideal pairs improves homodimer self-association and thermal stability. Unlike BECN1, all BECN2 CCD mutants bind ATG14, although more weakly than wild-type. Thus, polar BECN2 CCD interface residues result in a metastable homodimer, facilitating dissociation; but enable better interactions with polar ATG14 residues stabilizing the BECN2:ATG14 heterodimer. These structure-based mechanistic differences in BECN1 and BECN2 homodimerization and heterodimerization likely dictate competitive ATG14 recruitment. This article is protected by copyright. All rights reserved.
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| - | BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.,Su M, Li Y, Wyborny S, Neau D, Chakravarthy S, Levine B, Colbert CL, Sinha SC Protein Sci. 2017 Feb 20. doi: 10.1002/pro.3140. PMID:28218432<ref>PMID:28218432</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5k7b" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sinha, S]] | + | [[Category: Sinha S]] |
| - | [[Category: Su, M]] | + | [[Category: Su M]] |
| - | [[Category: Apoptosis]]
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| - | [[Category: Autophagy]]
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| - | [[Category: Coiled-coil domain]]
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| Structural highlights
Function
BECN2_HUMAN Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1.[1]
References
- ↑ He C, Wei Y, Sun K, Li B, Dong X, Zou Z, Liu Y, Kinch LN, Khan S, Sinha S, Xavier RJ, Grishin NV, Xiao G, Eskelinen EL, Scherer PE, Whistler JL, Levine B. Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism. Cell. 2013 Aug 29;154(5):1085-99. doi: 10.1016/j.cell.2013.07.035. Epub 2013 Aug , 15. PMID:23954414 doi:http://dx.doi.org/10.1016/j.cell.2013.07.035
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