|
|
| Line 3: |
Line 3: |
| <StructureSection load='3um3' size='340' side='right'caption='[[3um3]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='3um3' size='340' side='right'caption='[[3um3]], [[Resolution|resolution]] 3.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3um3]] is a 2 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=3UM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UM3 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3um3]] is a 2 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=3UM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UM3 FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r9m|3r9m]], [[3uly|3uly]], [[3um0|3um0]], [[3um1|3um1]], [[3um2|3um2]]</div></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BROFTI, BROX, C1orf58 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), C20orf178, CHMP4B, SHAX1 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3um3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3um3 OCA], [https://pdbe.org/3um3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3um3 RCSB], [https://www.ebi.ac.uk/pdbsum/3um3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3um3 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=3um3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3um3 OCA], [https://pdbe.org/3um3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3um3 RCSB], [https://www.ebi.ac.uk/pdbsum/3um3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3um3 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease ==
| |
| [[https://www.uniprot.org/uniprot/CHM4B_HUMAN CHM4B_HUMAN]] Defects in CHMP4B are the cause of cataract posterior polar type 3 (CTPP3) [MIM:[https://omim.org/entry/605387 605387]]. A subcapsular opacity, usually disk-shaped, located at the back of the lens. It can have a marked effect on visual acuity.<ref>PMID:17701905</ref>
| |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/CHM4B_HUMAN CHM4B_HUMAN]] Probable core 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. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:12860994</ref> <ref>PMID:14505569</ref> <ref>PMID:14505570</ref> <ref>PMID:14519844</ref> <ref>PMID:18209100</ref>
| | [https://www.uniprot.org/uniprot/BROX_HUMAN BROX_HUMAN] |
| <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>
| |
| <div class="pdbe-citations 3um3" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[Charged multivesicular body protein 3D structures|Charged multivesicular body protein 3D structures]] | | *[[Charged multivesicular body protein 3D structures|Charged multivesicular body protein 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Jiang, J S]] | | [[Category: Jiang JS]] |
| [[Category: Mu, R L]] | | [[Category: Mu RL]] |
| [[Category: Xiao, T]] | | [[Category: Xiao T]] |
| [[Category: Alpha-helix of c-terminal tail of chmp4b]]
| |
| [[Category: Brox]]
| |
| [[Category: Chmp]]
| |
| [[Category: Escrt-iii]]
| |
| [[Category: Membrane protein-transport protein complex]]
| |