3um0: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3um0]] 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=3UM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UM0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3um0]] 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=3UM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UM0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r9m|3r9m]], [[3uly|3uly]], [[3um1|3um1]], [[3um2|3um2]], [[3um3|3um3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r9m|3r9m]], [[3uly|3uly]], [[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])</td></tr> | <tr id='gene'><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])</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=3um0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3um0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3um0 RCSB], [http://www.ebi.ac.uk/pdbsum/3um0 PDBsum]</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=3um0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3um0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3um0 RCSB], [http://www.ebi.ac.uk/pdbsum/3um0 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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 | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Jiang, J S | [[Category: Jiang, J S]] | ||
[[Category: Mu, R L | [[Category: Mu, R L]] | ||
[[Category: Xiao, T | [[Category: Xiao, T]] | ||
[[Category: Beta hairpin]] | [[Category: Beta hairpin]] | ||
[[Category: Brox]] | [[Category: Brox]] | ||
Revision as of 13:36, 4 January 2015
Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP5Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail 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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