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5um3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the V122L mutant of human UBR-box domain from UBR2== | |
| - | + | <StructureSection load='5um3' size='340' side='right' caption='[[5um3]], [[Resolution|resolution]] 1.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5um3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UM3 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></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=5um3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5um3 OCA], [http://pdbe.org/5um3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5um3 RCSB], [http://www.ebi.ac.uk/pdbsum/5um3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5um3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/UBR2_HUMAN UBR2_HUMAN]] E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth.<ref>PMID:15548684</ref> <ref>PMID:20298436</ref> <ref>PMID:20835242</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: RING-type E3 ubiquitin transferase]] | ||
| + | [[Category: Escobar, J Munoz]] | ||
| + | [[Category: Gehring, K]] | ||
| + | [[Category: Kozlov, G]] | ||
| + | [[Category: Johansson blizard]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: N-end rule]] | ||
| + | [[Category: Ubr-box domain]] | ||
| + | [[Category: Zinc finger]] | ||
Revision as of 16:47, 22 March 2017
Crystal structure of the V122L mutant of human UBR-box domain from UBR2
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