3um3

From Proteopedia

(Difference between revisions)

Revision as of 07:46, 20 July 2022

Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP4B

Structural highlights

3um3 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3r9m, 3uly, 3um0, 3um1, 3um2
Gene:	BROFTI, BROX, C1orf58 (HUMAN), C20orf178, CHMP4B, SHAX1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CHM4B_HUMAN] Defects in CHMP4B are the cause of cataract posterior polar type 3 (CTPP3) [MIM:605387]. A subcapsular opacity, usually disk-shaped, located at the back of the lens. It can have a marked effect on visual acuity.^[1]

Function

[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.^[2] ^[3] ^[4] ^[5] ^[6]

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shiels A, Bennett TM, Knopf HL, Yamada K, Yoshiura K, Niikawa N, Shim S, Hanson PI. CHMP4B, a novel gene for autosomal dominant cataracts linked to chromosome 20q. Am J Hum Genet. 2007 Sep;81(3):596-606. Epub 2007 Jul 27. PMID:17701905 doi:S0002-9297(07)61356-1
↑ Katoh K, Shibata H, Suzuki H, Nara A, Ishidoh K, Kominami E, Yoshimori T, Maki M. The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J Biol Chem. 2003 Oct 3;278(40):39104-13. Epub 2003 Jul 14. PMID:12860994 doi:10.1074/jbc.M301604200
↑ Strack B, Calistri A, Craig S, Popova E, Gottlinger HG. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell. 2003 Sep 19;114(6):689-99. PMID:14505569
↑ von Schwedler UK, Stuchell M, Muller B, Ward DM, Chung HY, Morita E, Wang HE, Davis T, He GP, Cimbora DM, Scott A, Krausslich HG, Kaplan J, Morham SG, Sundquist WI. The protein network of HIV budding. Cell. 2003 Sep 19;114(6):701-13. PMID:14505570
↑ Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12414-9. Epub 2003 Sep 30. PMID:14519844 doi:10.1073/pnas.2133846100
↑ Hanson PI, Roth R, Lin Y, Heuser JE. Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. J Cell Biol. 2008 Jan 28;180(2):389-402. Epub 2008 Jan 21. PMID:18209100 doi:jcb.200707031
↑ Mu R, Dussupt V, Jiang J, Sette P, Rudd V, Chuenchor W, Bello NF, Bouamr F, Xiao TS. Two Distinct Binding Modes Define the Interaction of Brox with the C-Terminal Tails of CHMP5 and CHMP4B. Structure. 2012 May 9;20(5):887-98. Epub 2012 Apr 5. PMID:22484091 doi:10.1016/j.str.2012.03.001

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3um3"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP4B==
-<StructureSection load='3um3' size='340' side='right' caption='[[3um3]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+<StructureSection load='3um3' size='340' side='right'caption='[[3um3]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3um3]] is a 2 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=3UM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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/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>
-</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]], [[3um2|3um2]]</td></tr>
+</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>
-<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]), C20orf178, CHMP4B, SHAX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3um3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3um3 OCA], [http://pdbe.org/3um3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3um3 RCSB], [http://www.ebi.ac.uk/pdbsum/3um3 PDBsum], [http://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>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CHM4B_HUMAN CHM4B_HUMAN]] Defects in CHMP4B are the cause of cataract posterior polar type 3 (CTPP3) [MIM:[http://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>
+[[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 ==
-[[http://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/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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 </div>
 <div class="pdbe-citations 3um3" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Charged multivesicular body protein 3D structures|Charged multivesicular body protein 3D structures]]
 == References ==
 <references/>
@@ Line 26: / Line 29: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Jiang, J S]]
 [[Category: Mu, R L]]

3um3

From Proteopedia

Revision as of 07:46, 20 July 2022

Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP4B

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox