5nuv

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m (Protected "5nuv" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5nuv is ON HOLD until Paper Publication
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==Structure of the WD40-domain of human ATG16L1==
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<StructureSection load='5nuv' size='340' side='right' caption='[[5nuv]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5nuv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NUV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene></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=5nuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nuv OCA], [http://pdbe.org/5nuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nuv RCSB], [http://www.ebi.ac.uk/pdbsum/5nuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nuv ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/A16L1_HUMAN A16L1_HUMAN]] Crohn disease. Disease susceptibility is associated with variations affecting the gene represented in this entry.
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== Function ==
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[[http://www.uniprot.org/uniprot/A16L1_HUMAN A16L1_HUMAN]] Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II.<ref>PMID:23376921</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Autophagy-related protein ATG16L1 is a component of the mammalian ATG12 approximately ATG5/ATG16L1 complex, which acts as E3-ligase to catalyze lipidation of LC3 during autophagosome biogenesis. The N-terminal part of ATG16L1 comprises the ATG5-binding site and coiled-coil dimerization domain, both also present in yeast ATG16 and essential for bulk and starvation induced autophagy. While absent in yeast ATG16, mammalian ATG16L1 further contains a predicted C-terminal WD40-domain, which has been shown to be involved in mediating interaction with diverse factors in the context of alternative functions of autophagy, such as inflammatory control and xenophagy. In this work, we provide detailed information on the domain boundaries of the WD40-domain of human ATG16L1 and present its crystal structure at a resolution of 1.55 A.
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Authors:
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Structure of the WD40-domain of human ATG16L1.,Bajagic M, Archna A, Busing P, Scrima A Protein Sci. 2017 Sep;26(9):1828-1837. doi: 10.1002/pro.3222. Epub 2017 Jul 15. PMID:28685931<ref>PMID:28685931</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5nuv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bajagic, M]]
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[[Category: Scrima, A]]
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[[Category: Atg16l1]]
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[[Category: Protein binding]]
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[[Category: Seven-bladed beta-propeller]]
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[[Category: Wd40]]

Revision as of 03:47, 6 September 2017

Structure of the WD40-domain of human ATG16L1

5nuv, resolution 1.55Å

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