6rlb - Revision history

OCA at 10:12, 22 May 2024

OCA — Wed, 22 May 2024 10:12:35 GMT

←Older revision		Revision as of 10:12, 22 May 2024
Line 3:		Line 3:
	<SX load='6rlb' size='340' side='right' viewer='molstar' caption='[[6rlb]], [[Resolution\|resolution]] 4.50Å' scene=''>		<SX load='6rlb' size='340' side='right' viewer='molstar' caption='[[6rlb]], [[Resolution\|resolution]] 4.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6rlb]] is a 14 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=6RLB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6RLB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6rlb]] is a 14 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=6RLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RLB FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>WDR60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])~~, ~~WDR34 (~~[~~http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNC2LI1, D2LIC, LIC3, CGI-60 (~~[~~http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN~~]~~), DYNLRB1, BITH, DNCL2A, DNLC2A, ROBLD1, HSPC162 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN~~]~~), DYNLL1, DLC1, DNCL1, DNCLC1, HDLC1 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=~~5&~~id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 4.5Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [~~http~~://pdbe.org/6rlb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb 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=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [https://pdbe.org/6rlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [https://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/DC2L1_HUMAN DC2L1_HUMAN]] Jeune syndrome;Ellis Van Creveld syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/WDR34_HUMAN WDR34_HUMAN]] Short rib-polydactyly syndrome, Verma-Naumoff type;Jeune syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/WDR60_HUMAN WDR60_HUMAN]] Short rib-polydactyly syndrome, Verma-Naumoff type;Jeune syndrome. The disease is caused by mutations affecting the gene represented in this entry. Fibroblasts from affected individuals exhibit a defect in ciliogenesis and aberrant accumulation of the GLI2 transcription factor at the centrosome or basal body in the absence of an obvious axoneme.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~DYL1_HUMAN DYL1_HUMAN~~]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> [~~[http~~://www.uniprot.org/uniprot/~~DC2L1_HUMAN DC2L1_HUMAN~~]] Required for correct intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Involved in the regulation of ciliary length.<ref>PMID:26077881</ref> <ref>PMID:26130459</ref> [[http://www.uniprot.org/uniprot/WDR34_HUMAN WDR34_HUMAN]] Critical for ciliary functions, essential to normal development and survival, most probably as a previously unrecognized component of the mammalian dynein-motor-based intraflagellar transport (IFT) machinery. Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and 'Thr-187' upon Il-1 beta stimulation.<ref>PMID:19521662</ref> <ref>PMID:24183449</ref> [[http://www.uniprot.org/uniprot/WDR60_HUMAN WDR60_HUMAN]] May play a role in ciliogenesis.<ref>PMID:23910462</ref> [[http://www.uniprot.org/uniprot/DLRB1_HUMAN DLRB1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.	+	[https://www.uniprot.org/uniprot/B0I1S0_HUMAN B0I1S0_HUMAN] [https://www.uniprot.org/uniprot/E5BBQ0_HUMAN E5BBQ0_HUMAN]
	<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==
		+	*[[Dynein 3D structures\|Dynein 3D structures]]
	*[[WD-repeat protein 3D structures\|WD-repeat protein 3D structures]]		*[[WD-repeat protein 3D structures\|WD-repeat protein 3D structures]]
	== References ==		== References ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Carter~~, A P~~]]	+	[[Category: Carter AP]]
-	[[Category: Mladenov, M]]	+	[[Category: Mladenov M]]
-	[[Category: Mukhopadhyay~~, A G~~]]	+	[[Category: Mukhopadhyay AG]]
-	[[Category: Roberts~~, A J~~]]	+	[[Category: Roberts AJ]]
-	[[Category: Toropova, K]]	+	[[Category: Toropova K]]
-	[[Category: Zalyte, R]]	+	[[Category: Zalyte R]]
-	~~[[Category: Cilia]]~~	+
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Dynein]]~~	+
-	~~[[Category: Intraflagellar transport]]~~	+
-	~~[[Category: Motor protein~~]]	+

OCA at 05:45, 11 April 2020

OCA — Sat, 11 Apr 2020 05:45:41 GMT

←Older revision		Revision as of 05:45, 11 April 2020
Line 3:		Line 3:
	<SX load='6rlb' size='340' side='right' viewer='molstar' caption='[[6rlb]], [[Resolution\|resolution]] 4.50Å' scene=''>		<SX load='6rlb' size='340' side='right' viewer='molstar' caption='[[6rlb]], [[Resolution\|resolution]] 4.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6rlb]] is a 14 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=6RLB OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6RLB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6rlb]] is a 14 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=6RLB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RLB FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">WDR60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), WDR34 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNC2LI1, D2LIC, LIC3, CGI-60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNLRB1, BITH, DNCL2A, DNLC2A, ROBLD1, HSPC162 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNLL1, DLC1, DNCL1, DNCLC1, HDLC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">WDR60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), WDR34 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNC2LI1, D2LIC, LIC3, CGI-60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNLRB1, BITH, DNCL2A, DNLC2A, ROBLD1, HSPC162 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNLL1, DLC1, DNCL1, DNCLC1, HDLC1 ([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=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [http://pdbe.org/6rlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [http://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [http://pdbe.org/6rlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [http://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 6rlb" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6rlb" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[WD-repeat protein 3D structures\|WD-repeat protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 00:22, 7 March 2020

OCA — Sat, 07 Mar 2020 00:22:35 GMT

←Older revision		Revision as of 00:22, 7 March 2020
Line 1:		Line 1:

	==Structure of the dynein-2 complex; tail domain==		==Structure of the dynein-2 complex; tail domain==
-	<~~StructureSection~~ load='6rlb' size='340' side='right'caption='[[6rlb]], [[Resolution\|resolution]] 4.50Å' scene=''>	+	<SX load='6rlb' size='340' side='right' viewer='molstar' caption='[[6rlb]], [[Resolution\|resolution]] 4.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6rlb]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RLB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6rlb]] is a 14 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=6RLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RLB FirstGlance]. <br>
-	</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=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [http://pdbe.org/6rlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [http://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">WDR60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), WDR34 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNC2LI1, D2LIC, LIC3, CGI-60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNLRB1, BITH, DNCL2A, DNLC2A, ROBLD1, HSPC162 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DYNLL1, DLC1, DNCL1, DNCLC1, HDLC1 ([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=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [http://pdbe.org/6rlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [http://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DYL1_HUMAN DYL1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> [[http://www.uniprot.org/uniprot/DC2L1_HUMAN DC2L1_HUMAN]] Required for correct intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Involved in the regulation of ciliary length.<ref>PMID:26077881</ref> <ref>PMID:26130459</ref> [[http://www.uniprot.org/uniprot/WDR34_HUMAN WDR34_HUMAN]] Critical for ciliary functions, essential to normal development and survival, most probably as a previously unrecognized component of the mammalian dynein-motor-based intraflagellar transport (IFT) machinery. Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and 'Thr-187' upon Il-1 beta stimulation.<ref>PMID:19521662</ref> <ref>PMID:24183449</ref> [[http://www.uniprot.org/uniprot/WDR60_HUMAN WDR60_HUMAN]] May play a role in ciliogenesis.<ref>PMID:23910462</ref> [[http://www.uniprot.org/uniprot/DLRB1_HUMAN DLRB1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.		[[http://www.uniprot.org/uniprot/DYL1_HUMAN DYL1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> [[http://www.uniprot.org/uniprot/DC2L1_HUMAN DC2L1_HUMAN]] Required for correct intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Involved in the regulation of ciliary length.<ref>PMID:26077881</ref> <ref>PMID:26130459</ref> [[http://www.uniprot.org/uniprot/WDR34_HUMAN WDR34_HUMAN]] Critical for ciliary functions, essential to normal development and survival, most probably as a previously unrecognized component of the mammalian dynein-motor-based intraflagellar transport (IFT) machinery. Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and 'Thr-187' upon Il-1 beta stimulation.<ref>PMID:19521662</ref> <ref>PMID:24183449</ref> [[http://www.uniprot.org/uniprot/WDR60_HUMAN WDR60_HUMAN]] May play a role in ciliogenesis.<ref>PMID:23910462</ref> [[http://www.uniprot.org/uniprot/DLRB1_HUMAN DLRB1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60-WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60-WDR34-light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family.
		+
		+	Structure of the dynein-2 complex and its assembly with intraflagellar transport trains.,Toropova K, Zalyte R, Mukhopadhyay AG, Mladenov M, Carter AP, Roberts AJ Nat Struct Mol Biol. 2019 Sep;26(9):823-829. doi: 10.1038/s41594-019-0286-y. Epub, 2019 Aug 26. PMID:31451806<ref>PMID:31451806</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6rlb" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Carter, A P]]		[[Category: Carter, A P]]

OCA at 15:42, 28 August 2019

OCA — Wed, 28 Aug 2019 15:42:07 GMT

←Older revision		Revision as of 15:42, 28 August 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The entry ~~6rlb~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Structure of the dynein-2 complex; tail domain==
-		+	<StructureSection load='6rlb' size='340' side='right'caption='[[6rlb]], [[Resolution\|resolution]] 4.50Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6rlb]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RLB FirstGlance]. <br>
-	~~Description~~:	+	</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=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [http://pdbe.org/6rlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [http://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/DC2L1_HUMAN DC2L1_HUMAN]] Jeune syndrome;Ellis Van Creveld syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/WDR34_HUMAN WDR34_HUMAN]] Short rib-polydactyly syndrome, Verma-Naumoff type;Jeune syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/WDR60_HUMAN WDR60_HUMAN]] Short rib-polydactyly syndrome, Verma-Naumoff type;Jeune syndrome. The disease is caused by mutations affecting the gene represented in this entry. Fibroblasts from affected individuals exhibit a defect in ciliogenesis and aberrant accumulation of the GLI2 transcription factor at the centrosome or basal body in the absence of an obvious axoneme.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DYL1_HUMAN DYL1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> [[http://www.uniprot.org/uniprot/DC2L1_HUMAN DC2L1_HUMAN]] Required for correct intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Involved in the regulation of ciliary length.<ref>PMID:26077881</ref> <ref>PMID:26130459</ref> [[http://www.uniprot.org/uniprot/WDR34_HUMAN WDR34_HUMAN]] Critical for ciliary functions, essential to normal development and survival, most probably as a previously unrecognized component of the mammalian dynein-motor-based intraflagellar transport (IFT) machinery. Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and 'Thr-187' upon Il-1 beta stimulation.<ref>PMID:19521662</ref> <ref>PMID:24183449</ref> [[http://www.uniprot.org/uniprot/WDR60_HUMAN WDR60_HUMAN]] May play a role in ciliogenesis.<ref>PMID:23910462</ref> [[http://www.uniprot.org/uniprot/DLRB1_HUMAN DLRB1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Carter, A P]]
		+	[[Category: Mladenov, M]]
		+	[[Category: Mukhopadhyay, A G]]
		+	[[Category: Roberts, A J]]
		+	[[Category: Toropova, K]]
		+	[[Category: Zalyte, R]]
		+	[[Category: Cilia]]
		+	[[Category: Complex]]
		+	[[Category: Dynein]]
		+	[[Category: Intraflagellar transport]]
		+	[[Category: Motor protein]]

OCA at 04:53, 31 July 2019

OCA — Wed, 31 Jul 2019 04:53:11 GMT

←Older revision		Revision as of 04:53, 31 July 2019
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-	The entry 6rlb is ON HOLD	+	The entry 6rlb is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 04:38, 24 July 2019

OCA — Wed, 24 Jul 2019 04:38:24 GMT

←Older revision		Revision as of 04:38, 24 July 2019
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-	The entry 6rlb is ON HOLD ~~until sometime in the future~~	+	The entry 6rlb is ON HOLD

	Authors:		Authors:

OCA: Protected "6rlb" [edit=sysop:move=sysop]

OCA — Fri, 10 May 2019 08:31:16 GMT

Protected "6rlb" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:31, 10 May 2019

OCA: New page: '''Unreleased structure''' The entry 6rlb is ON HOLD until sometime in the future Authors: Description: Category: Unreleased Structures

OCA — Fri, 10 May 2019 08:31:14 GMT

New page: '''Unreleased structure''' The entry 6rlb is ON HOLD until sometime in the future Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6rlb is ON HOLD until sometime in the future

Authors:

Description:
[[Category: Unreleased Structures]]