5k7b: Difference between revisions

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'''Unreleased structure'''


The entry 5k7b is ON HOLD until Paper Publication
==Beclin 2 CCD homodimer==
<StructureSection load='5k7b' size='340' side='right' caption='[[5k7b]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5k7b]] is a 4 chain structure. 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>
</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>
</table>
== 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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5k7b" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Sinha, S]]
[[Category: Su, M]]
[[Category: Apoptosis]]
[[Category: Autophagy]]
[[Category: Coiled-coil domain]]
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