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3r9m

From Proteopedia

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Current revision (12:15, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3r9m' size='340' side='right'caption='[[3r9m]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3r9m' size='340' side='right'caption='[[3r9m]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r9m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R9M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r9m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R9M FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rau|3rau]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BROX, BROFTI, C1orf58 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9m OCA], [https://pdbe.org/3r9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r9m RCSB], [https://www.ebi.ac.uk/pdbsum/3r9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r9m ProSAT]</span></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=3r9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9m OCA], [https://pdbe.org/3r9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r9m RCSB], [https://www.ebi.ac.uk/pdbsum/3r9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r9m ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/BROX_HUMAN BROX_HUMAN]
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Alix and cellular paralogs HD-PTP and Brox contain N-terminal Bro1 domains that bind ESCRT-III CHMP4. In contrast to HD-PTP and Brox, expression of the Bro1 domain of Alix alleviates HIV-1 release defects as a result of interrupted access to ESCRT. In an attempt to elucidate this functional discrepancy, we solved the crystal structures of the Bro1 domains of HD-PTP and Brox. They revealed typical "boomerang" folds they share with the Bro1 Alix domain. However, they each contain unique structural features that may be relevant to their specific function(s). In particular, phenylalanine residue in position 105 (Phe105) of Alix belongs to a long loop that is unique to its Bro1 domain. Concurrently, mutation of Phe105 and surrounding residues at the tip of the loop compromise the function of Alix in HIV-1 budding without affecting its interactions with Gag or CHMP4. These studies identify a functional determinant in the Bro1 domain of Alix.
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The Phe105 Loop of Alix Bro1 Domain Plays a Key Role in HIV-1 Release.,Sette P, Mu R, Dussupt V, Jiang J, Snyder G, Smith P, Xiao TS, Bouamr F Structure. 2011 Sep 1. PMID:21889351<ref>PMID:21889351</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3r9m" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jiang, J S]]
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[[Category: Jiang JS]]
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[[Category: Mu, R L]]
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[[Category: Mu RL]]
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[[Category: Smith, P]]
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[[Category: Smith P]]
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[[Category: Snyder, G]]
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[[Category: Snyder G]]
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[[Category: Xiao, T]]
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[[Category: Xiao T]]
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[[Category: Bro1 domain]]
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[[Category: Protein binding]]
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Current revision

Crystal structure of the Brox Bro1 domain

PDB ID 3r9m

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