7sse - Revision history

OCA at 11:04, 22 November 2023

OCA — Wed, 22 Nov 2023 11:04:44 GMT

←Older revision		Revision as of 11:04, 22 November 2023
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DCAF1_HUMAN DCAF1_HUMAN] Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714).<ref>PMID:16964240</ref> <ref>PMID:17609381</ref> <ref>PMID:17630831</ref> <ref>PMID:18332868</ref> <ref>PMID:18524771</ref> <ref>PMID:18606781</ref> <ref>PMID:19287380</ref> <ref>PMID:20644714</ref> <ref>PMID:22184063</ref> <ref>PMID:23063525</ref> <ref>PMID:23362280</ref> <ref>PMID:24140421</ref> (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT.<ref>PMID:17314515</ref> <ref>PMID:17559673</ref> <ref>PMID:17609381</ref> <ref>PMID:17620334</ref> <ref>PMID:17626091</ref> <ref>PMID:17630831</ref> <ref>PMID:18524771</ref> <ref>PMID:24116224</ref> (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.<ref>PMID:17314515</ref> <ref>PMID:18464893</ref> <ref>PMID:19264781</ref> <ref>PMID:19923175</ref> <ref>PMID:24336198</ref>		[https://www.uniprot.org/uniprot/DCAF1_HUMAN DCAF1_HUMAN] Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714).<ref>PMID:16964240</ref> <ref>PMID:17609381</ref> <ref>PMID:17630831</ref> <ref>PMID:18332868</ref> <ref>PMID:18524771</ref> <ref>PMID:18606781</ref> <ref>PMID:19287380</ref> <ref>PMID:20644714</ref> <ref>PMID:22184063</ref> <ref>PMID:23063525</ref> <ref>PMID:23362280</ref> <ref>PMID:24140421</ref> (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT.<ref>PMID:17314515</ref> <ref>PMID:17559673</ref> <ref>PMID:17609381</ref> <ref>PMID:17620334</ref> <ref>PMID:17626091</ref> <ref>PMID:17630831</ref> <ref>PMID:18524771</ref> <ref>PMID:24116224</ref> (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.<ref>PMID:17314515</ref> <ref>PMID:18464893</ref> <ref>PMID:19264781</ref> <ref>PMID:19923175</ref> <ref>PMID:24336198</ref>
		+
		+	==See Also==
		+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:54, 18 October 2023

OCA — Wed, 18 Oct 2023 16:54:25 GMT

←Older revision		Revision as of 16:54, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='7sse' size='340' side='right'caption='[[7sse]], [[Resolution\|resolution]] 1.62Å' scene=''>		<StructureSection load='7sse' size='340' side='right'caption='[[7sse]], [[Resolution\|resolution]] 1.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7sse]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SSE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7sse]] 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=7SSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SSE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=B1I:N~~-[~~(3R)-~~1~~-(3-fluorophenyl)piperidin-3-yl]-6-(morpholin-4-yl)pyrimidin-4-amine'>B1I</scene>~~</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]] 1.62Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Non~~-~~specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number~~ [~~https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.~~1] </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1I:N-[(3R)-1-(3-fluorophenyl)piperidin-3-yl]-6-(morpholin-4-yl)pyrimidin-4-amine'>B1I</scene></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=7sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sse OCA], [https://pdbe.org/7sse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sse RCSB], [https://www.ebi.ac.uk/pdbsum/7sse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sse 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=7sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sse OCA], [https://pdbe.org/7sse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sse RCSB], [https://www.ebi.ac.uk/pdbsum/7sse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sse ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DCAF1_HUMAN DCAF1_HUMAN]] Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714).<ref>PMID:16964240</ref> <ref>PMID:17609381</ref> <ref>PMID:17630831</ref> <ref>PMID:18332868</ref> <ref>PMID:18524771</ref> <ref>PMID:18606781</ref> <ref>PMID:19287380</ref> <ref>PMID:20644714</ref> <ref>PMID:22184063</ref> <ref>PMID:23063525</ref> <ref>PMID:23362280</ref> <ref>PMID:24140421</ref> (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT.<ref>PMID:17314515</ref> <ref>PMID:17559673</ref> <ref>PMID:17609381</ref> <ref>PMID:17620334</ref> <ref>PMID:17626091</ref> <ref>PMID:17630831</ref> <ref>PMID:18524771</ref> <ref>PMID:24116224</ref> (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.<ref>PMID:17314515</ref> <ref>PMID:18464893</ref> <ref>PMID:19264781</ref> <ref>PMID:19923175</ref> <ref>PMID:24336198</ref>	+	[https://www.uniprot.org/uniprot/DCAF1_HUMAN DCAF1_HUMAN] Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714).<ref>PMID:16964240</ref> <ref>PMID:17609381</ref> <ref>PMID:17630831</ref> <ref>PMID:18332868</ref> <ref>PMID:18524771</ref> <ref>PMID:18606781</ref> <ref>PMID:19287380</ref> <ref>PMID:20644714</ref> <ref>PMID:22184063</ref> <ref>PMID:23063525</ref> <ref>PMID:23362280</ref> <ref>PMID:24140421</ref> (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT.<ref>PMID:17314515</ref> <ref>PMID:17559673</ref> <ref>PMID:17609381</ref> <ref>PMID:17620334</ref> <ref>PMID:17626091</ref> <ref>PMID:17630831</ref> <ref>PMID:18524771</ref> <ref>PMID:24116224</ref> (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.<ref>PMID:17314515</ref> <ref>PMID:18464893</ref> <ref>PMID:19264781</ref> <ref>PMID:19923175</ref> <ref>PMID:24336198</ref>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Arrowsmith CH]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Dong A]]
-	[[Category: Dong, A]]	+	[[Category: Edwards AM]]
-	[[Category: Edwards~~, A M~~]]	+	[[Category: Halabelian L]]
-	[[Category: Halabelian, L]]	+	[[Category: Hutchinson A]]
-	[[Category: Hutchinson, A]]	+	[[Category: Kimani S]]
-	[[Category: Kimani, S]]	+	[[Category: Li A]]
-	[[Category: Li, A]]	+	[[Category: Li Y]]
-	[[Category: Li, Y]]	+	[[Category: Owen J]]
-	[[Category: Owen, J]]	+	[[Category: Schapira M]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Seitova A]]
-	[[Category: Schapira, M]]	+	[[Category: Shahani VM]]
-	[[Category: Seitova, A]]	+
-	[[Category: Shahani~~, V M]]~~	+
-	~~[[Category: Dcaf1]]~~	+
-	~~[[Category: Sgc]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Wd-repeat]]~~	+
-	~~[[Category: Wdr~~]]	+

OCA at 08:45, 23 February 2022

OCA — Wed, 23 Feb 2022 08:45:40 GMT

←Older revision		Revision as of 08:45, 23 February 2022
Line 1:		Line 1:

	==Crystal structure of the WDR domain of human DCAF1 in complex with CYCA-117-70==		==Crystal structure of the WDR domain of human DCAF1 in complex with CYCA-117-70==
-	<StructureSection load='7sse' size='340' side='right'caption='[[7sse]]' scene=''>	+	<StructureSection load='7sse' size='340' side='right'caption='[[7sse]], [[Resolution\|resolution]] 1.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SSE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7sse]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SSE 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=7sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sse OCA], [https://pdbe.org/7sse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sse RCSB], [https://www.ebi.ac.uk/pdbsum/7sse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sse ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1I:N-[(3R)-1-(3-fluorophenyl)piperidin-3-yl]-6-(morpholin-4-yl)pyrimidin-4-amine'>B1I</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=7sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sse OCA], [https://pdbe.org/7sse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sse RCSB], [https://www.ebi.ac.uk/pdbsum/7sse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sse ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/DCAF1_HUMAN DCAF1_HUMAN]] Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714).<ref>PMID:16964240</ref> <ref>PMID:17609381</ref> <ref>PMID:17630831</ref> <ref>PMID:18332868</ref> <ref>PMID:18524771</ref> <ref>PMID:18606781</ref> <ref>PMID:19287380</ref> <ref>PMID:20644714</ref> <ref>PMID:22184063</ref> <ref>PMID:23063525</ref> <ref>PMID:23362280</ref> <ref>PMID:24140421</ref> (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT.<ref>PMID:17314515</ref> <ref>PMID:17559673</ref> <ref>PMID:17609381</ref> <ref>PMID:17620334</ref> <ref>PMID:17626091</ref> <ref>PMID:17630831</ref> <ref>PMID:18524771</ref> <ref>PMID:24116224</ref> (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.<ref>PMID:17314515</ref> <ref>PMID:18464893</ref> <ref>PMID:19264781</ref> <ref>PMID:19923175</ref> <ref>PMID:24336198</ref>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arrowsmith CH]]	+	[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Dong A]]	+	[[Category: Arrowsmith, C H]]
-	[[Category: Edwards AM]]	+	[[Category: Dong, A]]
-	[[Category: Halabelian L]]	+	[[Category: Edwards, A M]]
-	[[Category: Hutchinson A]]	+	[[Category: Halabelian, L]]
-	[[Category: Kimani S]]	+	[[Category: Hutchinson, A]]
-	[[Category: Li Y]]	+	[[Category: Kimani, S]]
-	[[Category: Owen J]]	+	[[Category: Li, A]]
-	[[Category: Schapira M]]	+	[[Category: Li, Y]]
-	[[Category: Seitova A]]	+	[[Category: Owen, J]]
-	[[Category: Shahani VM]]	+	[[Category: Structural genomic]]
		+	[[Category: Schapira, M]]
		+	[[Category: Seitova, A]]
		+	[[Category: Shahani, V M]]
		+	[[Category: Dcaf1]]
		+	[[Category: Sgc]]
		+	[[Category: Transferase]]
		+	[[Category: Wd-repeat]]
		+	[[Category: Wdr]]

OCA at 16:50, 15 December 2021

OCA — Wed, 15 Dec 2021 16:50:56 GMT

←Older revision		Revision as of 16:50, 15 December 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7sse ~~is ON HOLD~~	+	==Crystal structure of the WDR domain of human DCAF1 in complex with CYCA-117-70==
-		+	<StructureSection load='7sse' size='340' side='right'caption='[[7sse]]' scene=''>
-	~~Authors~~: ~~Kimani, S~~.~~, Owen, J~~.~~, Dong, A~~.~~, Li, Y~~.~~, Hutchinson, A~~.~~, Seitova, A~~.~~, Shahani, V~~.M.~~, Schapira, M~~., ~~Arrowsmith, C~~.H., ~~Edwards~~, A.M., ~~Halabelian~~, L.~~, Structural Genomics Consortium (SGC)~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SSE FirstGlance]. <br>
-	~~Description: Crystal structure of the WDR domain of human DCAF1 in complex with CYCA-117-70~~	+	</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=7sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sse OCA], [https://pdbe.org/7sse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sse RCSB], [https://www.ebi.ac.uk/pdbsum/7sse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sse ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Hutchinson, A~~]]	+	__TOC__
-	[[Category: ~~Owen, J~~]]	+	</StructureSection>
-	[[Category: ~~Arrowsmith, C.H~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Seitova, A~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: ~~Dong,~~ A]]	+	[[Category: Dong A]]
-	[[Category: ~~Li, Y~~]]	+	[[Category: Edwards AM]]
-	[[Category: ~~Halabelian, L~~]]	+	[[Category: Halabelian L]]
-	[[Category: ~~Shahani, V.M~~]]	+	[[Category: Hutchinson A]]
-	[[Category: Schapira, M]]	+	[[Category: Kimani S]]
-	[[Category: ~~Edwards,~~ A.M]]	+	[[Category: Li Y]]
-	[[Category: ~~Structural Genomics Consortium (Sgc)]]~~	+	[[Category: Owen J]]
-	~~[[Category: Kimani, S~~]]	+	[[Category: Schapira M]]
		+	[[Category: Seitova A]]
		+	[[Category: Shahani VM]]

OCA: Protected "7sse" [edit=sysop:move=sysop]

OCA — Wed, 17 Nov 2021 12:16:18 GMT

Protected "7sse" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:16, 17 November 2021

OCA: New page: '''Unreleased structure''' The entry 7sse is ON HOLD Authors: Kimani, S., Owen, J., Dong, A., Li, Y., Hutchinson, A., Seitova, A., Shahani, V.M., Schapira, M., Arrowsmith, C.H., Edwards...

OCA — Wed, 17 Nov 2021 12:16:17 GMT

New page: '''Unreleased structure''' The entry 7sse is ON HOLD Authors: Kimani, S., Owen, J., Dong, A., Li, Y., Hutchinson, A., Seitova, A., Shahani, V.M., Schapira, M., Arrowsmith, C.H., Edwards...

New page

'''Unreleased structure'''

The entry 7sse is ON HOLD

Authors: Kimani, S., Owen, J., Dong, A., Li, Y., Hutchinson, A., Seitova, A., Shahani, V.M., Schapira, M., Arrowsmith, C.H., Edwards, A.M., Halabelian, L., Structural Genomics Consortium (SGC)

Description: Crystal structure of the WDR domain of human DCAF1 in complex with CYCA-117-70
[[Category: Unreleased Structures]]
[[Category: Hutchinson, A]]
[[Category: Owen, J]]
[[Category: Arrowsmith, C.H]]
[[Category: Seitova, A]]
[[Category: Dong, A]]
[[Category: Li, Y]]
[[Category: Halabelian, L]]
[[Category: Shahani, V.M]]
[[Category: Schapira, M]]
[[Category: Edwards, A.M]]
[[Category: Structural Genomics Consortium (Sgc)]]
[[Category: Kimani, S]]