3um2
From Proteopedia
(Difference between revisions)
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==Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP5== | ==Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP5== | ||
<StructureSection load='3um2' size='340' side='right' caption='[[3um2]], [[Resolution|resolution]] 2.59Å' scene=''> | <StructureSection load='3um2' size='340' side='right' caption='[[3um2]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3um2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3um2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UM2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UM2 FirstGlance]. <br> |
</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> | </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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r9m|3r9m]], [[3uly|3uly]], [[3um0|3um0]], [[3um1|3um1]], [[3um3|3um3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r9m|3r9m]], [[3uly|3uly]], [[3um0|3um0]], [[3um1|3um1]], [[3um3|3um3]]</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 | + | <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 HUMAN])</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=3um2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3um2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3um2 RCSB], [http://www.ebi.ac.uk/pdbsum/3um2 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=3um2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3um2 OCA], [http://pdbe.org/3um2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3um2 RCSB], [http://www.ebi.ac.uk/pdbsum/3um2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3um2 ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CHMP5_HUMAN CHMP5_HUMAN]] Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 3um2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Human]] |
[[Category: Jiang, J S]] | [[Category: Jiang, J S]] | ||
[[Category: Mu, R L]] | [[Category: Mu, R L]] |
Revision as of 20:52, 11 August 2016
Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP5
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