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[[ | ==Crystal Structure of BROX Bro1 Domain in Complex with the C-Terminal Tails of CHMP5== | ||
<StructureSection load='3uly' size='340' side='right' caption='[[3uly]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3uly]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ULY FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r9m|3r9m]], [[3um0|3um0]], [[3um1|3um1]], [[3um2|3um2]], [[3um3|3um3]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BROFTI, BROX, C1orf58 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), C9orf83, CGI-34, CHMP5, HSPC177, PNAS-114, PNAS-2, SNF7DC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3uly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uly OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uly RCSB], [http://www.ebi.ac.uk/pdbsum/3uly PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Interactions of the CHMP protein carboxyl terminal tails with effector proteins play important roles in retroviral budding, cytokinesis, and multivesicular body biogenesis. Here we demonstrate that hydrophobic residues at the CHMP4B C-terminal amphipathic alpha helix bind a concave surface of Brox, a mammalian paralog of Alix. Unexpectedly, CHMP5 was also found to bind Brox and specifically recruit endogenous Brox to detergent-resistant membrane fractions through its C-terminal 20 residues. Instead of an alpha helix, the CHMP5 C-terminal tail adopts a tandem beta-hairpin structure that binds Brox at the same site as CHMP4B. Additional Brox:CHMP5 interface is furnished by a unique CHMP5 hydrophobic pocket engaging the Brox residue Y348 that is not conserved among the Bro1 domains. Our studies thus unveil a beta-hairpin conformation of the CHMP5 protein C-terminal tail, and provide insights into the overlapping but distinct binding profiles of ESCRT-III and the Bro1 domain proteins. | |||
Two Distinct Binding Modes Define the Interaction of Brox with the C-Terminal Tails of CHMP5 and CHMP4B.,Mu R, Dussupt V, Jiang J, Sette P, Rudd V, Chuenchor W, Bello NF, Bouamr F, Xiao TS Structure. 2012 May 9;20(5):887-98. Epub 2012 Apr 5. PMID:22484091<ref>PMID:22484091</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Jiang, J S.]] | [[Category: Jiang, J S.]] | ||
Revision as of 09:26, 5 June 2014
Crystal Structure of BROX Bro1 Domain in Complex with the C-Terminal Tails of CHMP5Crystal Structure of BROX Bro1 Domain in Complex with the C-Terminal Tails of CHMP5
Structural highlights
Publication Abstract from PubMedInteractions of the CHMP protein carboxyl terminal tails with effector proteins play important roles in retroviral budding, cytokinesis, and multivesicular body biogenesis. Here we demonstrate that hydrophobic residues at the CHMP4B C-terminal amphipathic alpha helix bind a concave surface of Brox, a mammalian paralog of Alix. Unexpectedly, CHMP5 was also found to bind Brox and specifically recruit endogenous Brox to detergent-resistant membrane fractions through its C-terminal 20 residues. Instead of an alpha helix, the CHMP5 C-terminal tail adopts a tandem beta-hairpin structure that binds Brox at the same site as CHMP4B. Additional Brox:CHMP5 interface is furnished by a unique CHMP5 hydrophobic pocket engaging the Brox residue Y348 that is not conserved among the Bro1 domains. Our studies thus unveil a beta-hairpin conformation of the CHMP5 protein C-terminal tail, and provide insights into the overlapping but distinct binding profiles of ESCRT-III and the Bro1 domain proteins. Two Distinct Binding Modes Define the Interaction of Brox with the C-Terminal Tails of CHMP5 and CHMP4B.,Mu R, Dussupt V, Jiang J, Sette P, Rudd V, Chuenchor W, Bello NF, Bouamr F, Xiao TS Structure. 2012 May 9;20(5):887-98. Epub 2012 Apr 5. PMID:22484091[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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