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5k9l

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==Beclin 2 CCD N187L mutant homodimer==
==Beclin 2 CCD N187L mutant homodimer==
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<StructureSection load='5k9l' size='340' side='right' caption='[[5k9l]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
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<StructureSection load='5k9l' size='340' side='right'caption='[[5k9l]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5k9l]] 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=5K9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K9L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5k9l]] 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=5K9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K9L FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52&#8491;</td></tr>
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<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=5k9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9l OCA], [http://pdbe.org/5k9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9l RCSB], [http://www.ebi.ac.uk/pdbsum/5k9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9l ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9l OCA], [https://pdbe.org/5k9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k9l RCSB], [https://www.ebi.ac.uk/pdbsum/5k9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5k9l" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Sinha, S]]
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[[Category: Large Structures]]
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[[Category: Su, M]]
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[[Category: Sinha S]]
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[[Category: Apoptosis]]
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[[Category: Su M]]
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[[Category: Autophagy]]
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[[Category: Coiled-coil domain]]
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Current revision

Beclin 2 CCD N187L mutant homodimer

PDB ID 5k9l

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