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| | <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 == |
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| | __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]]
| + | |
