4txq - Revision history

OCA at 07:24, 27 September 2023

OCA — Wed, 27 Sep 2023 07:24:06 GMT

←Older revision		Revision as of 07:24, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4txq]] is a 4 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=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4txq]] is a 4 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=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>
-	</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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [https://pdbe.org/4txq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [https://www.ebi.ac.uk/pdbsum/4txq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4txq ProSAT]</span></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]] 2.21Å</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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [https://pdbe.org/4txq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [https://www.ebi.ac.uk/pdbsum/4txq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4txq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 07:51, 22 March 2023

OCA — Wed, 22 Mar 2023 07:51:22 GMT

←Older revision		Revision as of 07:51, 22 March 2023
Line 3:		Line 3:
	<StructureSection load='4txq' size='340' side='right'caption='[[4txq]], [[Resolution\|resolution]] 2.21Å' scene=''>		<StructureSection load='4txq' size='340' side='right'caption='[[4txq]], [[Resolution\|resolution]] 2.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4txq]] 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=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4txq]] is a 4 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=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4txp\|4txp]], [[4txr\|4txr]]</td></tr>~~	+	</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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [https://pdbe.org/4txq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [https://www.ebi.ac.uk/pdbsum/4txq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4txq ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VTA1, C6orf55, HSPC228, My012 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CHMP1B, C18orf2 ([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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [~~http~~://pdbe.org/4txq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4txq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4txq ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/VTA1_HUMAN VTA1_HUMAN]] Involved in the endosomal multivesicular bodies (MVB) pathway. 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. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.<ref>PMID:15644320</ref> [[http://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_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 cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>	+	[https://www.uniprot.org/uniprot/VTA1_HUMAN VTA1_HUMAN] Involved in the endosomal multivesicular bodies (MVB) pathway. 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. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.<ref>PMID:15644320</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==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]]
-	*[[Vacuolar protein sorting-associated protein\|Vacuolar protein sorting-associated protein]]	+	*[[Vacuolar protein sorting-associated protein 3D structures\|Vacuolar protein sorting-associated protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Vild~~, C J~~]]	+	[[Category: Vild CJ]]
-	[[Category: Xu, Z]]	+	[[Category: Xu Z]]
-	~~[[Category: Escrt]]~~	+
-	~~[[Category: Mit]]~~	+
-	~~[[Category: Mit domain]]~~	+
-	~~[[Category: Protein transport~~]]	+

OCA at 14:45, 10 May 2019

OCA — Fri, 10 May 2019 14:45:05 GMT

←Older revision		Revision as of 14:45, 10 May 2019
Line 1:		Line 1:

	==Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM==		==Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM==
-	<StructureSection load='4txq' size='340' side='right' caption='[[4txq]], [[Resolution\|resolution]] 2.21Å' scene=''>	+	<StructureSection load='4txq' size='340' side='right'caption='[[4txq]], [[Resolution\|resolution]] 2.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4txq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4txq]] 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=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4txp\|4txp]], [[4txr\|4txr]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4txp\|4txp]], [[4txr\|4txr]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VTA1, C6orf55, HSPC228, My012 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CHMP1B, C18orf2 ([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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [http://pdbe.org/4txq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [http://www.ebi.ac.uk/pdbsum/4txq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4txq ProSAT]</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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [http://pdbe.org/4txq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [http://www.ebi.ac.uk/pdbsum/4txq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4txq ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4txq" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4txq" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Charged multivesicular body protein 3D structures\|Charged multivesicular body protein 3D structures]]
		+	*[[Vacuolar protein sorting-associated protein\|Vacuolar protein sorting-associated protein]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Vild, C J]]		[[Category: Vild, C J]]
	[[Category: Xu, Z]]		[[Category: Xu, Z]]

OCA at 01:11, 19 January 2017

OCA — Thu, 19 Jan 2017 01:11:01 GMT

←Older revision		Revision as of 01:11, 19 January 2017
Line 1:		Line 1:
		+
	==Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM==		==Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM==
	<StructureSection load='4txq' size='340' side='right' caption='[[4txq]], [[Resolution\|resolution]] 2.21Å' scene=''>		<StructureSection load='4txq' size='340' side='right' caption='[[4txq]], [[Resolution\|resolution]] 2.21Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4txq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4txq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4txp\|4txp]], [[4txr\|4txr]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4txp\|4txp]], [[4txr\|4txr]]</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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [http://www.ebi.ac.uk/pdbsum/4txq 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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [http://pdbe.org/4txq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [http://www.ebi.ac.uk/pdbsum/4txq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4txq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4txq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:23, 18 February 2015

OCA — Wed, 18 Feb 2015 07:23:22 GMT

←Older revision		Revision as of 07:23, 18 February 2015
Line 8:		Line 8:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/VTA1_HUMAN VTA1_HUMAN]] Involved in the endosomal multivesicular bodies (MVB) pathway. 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. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.<ref>PMID:15644320</ref> [[http://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_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 cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>		[[http://www.uniprot.org/uniprot/VTA1_HUMAN VTA1_HUMAN]] Involved in the endosomal multivesicular bodies (MVB) pathway. 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. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.<ref>PMID:15644320</ref> [[http://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_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 cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Disassembly of the endosomal sorting complex required for transport (ESCRT) machinery from biological membranes is a critical final step in cellular processes that require the ESCRT function. This reaction is catalyzed by VPS4, a AAA-ATPase whose activity is tightly regulated by a host of proteins including LIP5 and the ESCRT-III proteins. Here, we present structural and functional analyses of molecular interactions between human VPS4, LIP5 and the ESCRT-III proteins. The N-terminal domain of LIP5 (LIP5NTD) is required for LIP5-mediated stimulation of VPS4 and the ESCRT-III protein CHMP5 strongly inhibits the stimulation. Both of these observations are distinct from what was previously described for homologous yeast proteins. The crystal structure of LIP5NTD in complex with the MIT-interacting motifs (MIMs) of CHMP5 and a second ESCRT-III protein CHMP1B was determined at 1 angstrom resolution. It reveals an ESCRT-III binding induced moderate conformational change in LIP5NTD, which results from insertion of a conserved CHMP5 tyrosine residue (Tyr182) at the core of LIP5NTD structure. Mutation of Tyr182 partially relieves the inhibition displayed by CHMP5. Together, these results suggest a novel mechanism of VPS4 regulation in metazoans, where CHMP5 functions as a negative allosteric switch to control LIP5-mediated stimulation of VPS4.
		+
		+	A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5.,Vild CJ, Li Y, Guo EZ, Liu Y, Xu Z J Biol Chem. 2015 Jan 30. pii: jbc.M114.616730. PMID:25637630<ref>PMID:25637630</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:01, 12 February 2015

OCA — Thu, 12 Feb 2015 12:01:19 GMT

←Older revision		Revision as of 12:01, 12 February 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM==
-		+	<StructureSection load='4txq' size='340' side='right' caption='[[4txq]], [[Resolution\|resolution]] 2.21Å' scene=''>
-	~~The entry~~ 4txq is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4txq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TXQ FirstGlance]. <br>
-	~~Authors~~: ~~Vild~~, C.J., Xu, Z.	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4txp\|4txp]], [[4txr\|4txr]]</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=4txq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4txq RCSB], [http://www.ebi.ac.uk/pdbsum/4txq PDBsum]</span></td></tr>
-	~~Description~~: ~~Crystal structure~~ of ~~LIP5 N~~-terminal ~~domain complexed~~ with ~~CHMP1B MIM~~	+	</table>
-	[[Category: ~~Unreleased Structures~~]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VTA1_HUMAN VTA1_HUMAN]] Involved in the endosomal multivesicular bodies (MVB) pathway. 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. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.<ref>PMID:15644320</ref> [[http://www.uniprot.org/uniprot/CHM1B_HUMAN CHM1B_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 cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14519844</ref> <ref>PMID:19129479</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Vild, C J]]
	[[Category: Xu, Z]]		[[Category: Xu, Z]]
-	[[Category: ~~Vild, C.J~~]]	+	[[Category: Escrt]]
		+	[[Category: Mit]]
		+	[[Category: Mit domain]]
		+	[[Category: Protein transport]]

OCA at 17:57, 24 December 2014

OCA — Wed, 24 Dec 2014 17:57:57 GMT

←Older revision		Revision as of 17:57, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM		Description: Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM
		+	[[Category: Unreleased Structures]]
		+	[[Category: Xu, Z]]
		+	[[Category: Vild, C.J]]

OCA: Protected "4txq" [edit=sysop:move=sysop]

OCA — Wed, 16 Jul 2014 09:56:46 GMT

Protected "4txq" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:56, 16 July 2014

OCA: New page: '''Unreleased structure''' The entry 4txq is ON HOLD until Paper Publication Authors: Vild, C.J., Xu, Z. Description: Crystal structure of LIP5 N-terminal domain complexed with CHMP1B ...

OCA — Wed, 16 Jul 2014 09:56:45 GMT

New page: '''Unreleased structure''' The entry 4txq is ON HOLD until Paper Publication Authors: Vild, C.J., Xu, Z. Description: Crystal structure of LIP5 N-terminal domain complexed with CHMP1B ...

New page

'''Unreleased structure'''

The entry 4txq is ON HOLD until Paper Publication

Authors: Vild, C.J., Xu, Z.

Description: Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM