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5im8
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of the Microtubule-Targeting COS Domain of MID1== | |
| + | <StructureSection load='5im8' size='340' side='right'caption='[[5im8]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5im8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IM8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5im8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5im8 OCA], [https://pdbe.org/5im8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5im8 RCSB], [https://www.ebi.ac.uk/pdbsum/5im8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5im8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/TRI18_HUMAN TRI18_HUMAN] Defects in MID1 are the cause of Opitz GBBB syndrome 1 (OGS1) [MIM:[https://omim.org/entry/300000 300000]. A congenital midline malformation syndrome characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. Note=MID1 mutations produce proteins with a decreased affinity for microtubules.<ref>PMID:9354791</ref> <ref>PMID:11030761</ref> <ref>PMID:9718340</ref> <ref>PMID:15558842</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRI18_HUMAN TRI18_HUMAN] Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination.<ref>PMID:10400985</ref> <ref>PMID:11685209</ref> <ref>PMID:22613722</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The human MID1 protein is required for the proper development during embryogenesis. Mutations of MID1 are associated with X-linked Opitz G syndrome, characterized by midline anomalies. MID1 associates with the microtubules and functions as an ubiquitin E3 ligase, targeting protein phosphatase 2A for ubiquitin-mediated regulation. The mechanism of microtubule association is not known. Recently, a 60-amino acid region termed the COS box/domain was identified at the C-terminal end of the coiled-coil (CC) domain that facilitates microtubule localization. Insertion of the MID1 COS domain at the C-terminal end of the CC domain of a non-microtubule associated TRIM protein confers microtubule localization. Here, we report the solution structure of the COS domain of MID1. The domain adopts a helix-loop-helix structure in which the N- and C-terminal ends are in close proximity. Hydrophobic residues stabilizing the interaction of the two alpha-helices form a central hydrophobic core. The loop separating the alpha-helices is structured, with two of its hydrophobic residues making contact with the central core. On the outer surface, positively charged residues form a distinct basic patch near the termini that we postulate is important for microtubule binding. A model of the structure of the preceding coiled-coil and COS domains (CC-COS) show that the COS domain forms a helical bundle at the C-terminal end of the CC domain similar to the spectrin-like fold observed with some known microtubule-binding proteins. Interestingly, the CC-COS domains bind to microtubules, demonstrating for the first time that MID1 can directly associate with the microtubules. This article is protected by copyright. All rights reserved. | ||
| - | + | Solution Structure of the Microtubule-Targeting COS Domain of MID1.,Wright KM, Du H, Dagnachew M, Massiah MA FEBS J. 2016 Jul 1. doi: 10.1111/febs.13795. PMID:27367845<ref>PMID:27367845</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5im8" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dagnachew M]] | ||
| + | [[Category: Du H]] | ||
| + | [[Category: Massiah MA]] | ||
| + | [[Category: Wright KM]] | ||
Current revision
Solution Structure of the Microtubule-Targeting COS Domain of MID1
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