6dce

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'''Unreleased structure'''
 
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The entry 6dce is ON HOLD until Paper Publication
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==X-ray structure of FIP200 claw domain==
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<StructureSection load='6dce' size='340' side='right' caption='[[6dce]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
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Authors: Su, M.-Y., Hurley, J.H.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6dce]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DCE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DCE FirstGlance]. <br>
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Description: X-ray structure of FIP200 claw domain
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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[[Category: Su, M.-Y]]
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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=6dce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dce OCA], [http://pdbe.org/6dce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dce RCSB], [http://www.ebi.ac.uk/pdbsum/6dce PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dce ProSAT]</span></td></tr>
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[[Category: Hurley, J.H]]
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/RBCC1_HUMAN RBCC1_HUMAN]] Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity).[UniProtKB:Q9ESK9]<ref>PMID:10769033</ref> <ref>PMID:12095676</ref> <ref>PMID:12163359</ref> <ref>PMID:12221124</ref> <ref>PMID:14533007</ref> <ref>PMID:21775823</ref> <ref>PMID:23392225</ref>
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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: Hurley, J H]]
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[[Category: Su, M Y]]
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[[Category: Autophagy]]
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[[Category: Fip200]]
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[[Category: Structural protein]]

Revision as of 07:27, 6 March 2019

X-ray structure of FIP200 claw domain

6dce, resolution 1.56Å

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