5aja - Revision history

OCA at 11:10, 10 January 2024

OCA — Wed, 10 Jan 2024 11:10:46 GMT

←Older revision		Revision as of 11:10, 10 January 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5aja]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mandrillus_sphinx Mandrillus sphinx] and [https://en.wikipedia.org/wiki/Simian_immunodeficiency_virus Simian immunodeficiency virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AJA FirstGlance]. <br>		<table><tr><td colspan='2'>[[5aja]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mandrillus_sphinx Mandrillus sphinx] and [https://en.wikipedia.org/wiki/Simian_immunodeficiency_virus Simian immunodeficiency virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AJA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.649Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5aja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aja OCA], [https://pdbe.org/5aja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aja RCSB], [https://www.ebi.ac.uk/pdbsum/5aja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aja 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=5aja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aja OCA], [https://pdbe.org/5aja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aja RCSB], [https://www.ebi.ac.uk/pdbsum/5aja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aja ProSAT]</span></td></tr>
	</table>		</table>

OCA at 05:03, 25 May 2023

OCA — Thu, 25 May 2023 05:03:46 GMT

←Older revision		Revision as of 05:03, 25 May 2023
Line 3:		Line 3:
	<StructureSection load='5aja' size='340' side='right'caption='[[5aja]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='5aja' size='340' side='right'caption='[[5aja]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5aja]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Civ Civ~~], [~~http~~://en.wikipedia.org/wiki/~~Human Human~~] and [~~http~~://en.wikipedia.org/wiki/~~Mansp Mansp~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5AJA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5aja]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mandrillus_sphinx Mandrillus sphinx] and [https://en.wikipedia.org/wiki/Simian_immunodeficiency_virus Simian immunodeficiency virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AJA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://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=5aja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aja OCA], [https://pdbe.org/5aja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aja RCSB], [https://www.ebi.ac.uk/pdbsum/5aja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aja 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=5aja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aja OCA], [~~http~~://pdbe.org/5aja PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5aja RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5aja PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5aja ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~VPRBP_HUMAN VPRBP_HUMAN~~]~~] Component~~ of ~~the CUL4A~~-~~RBX1~~-DDB1-~~VprBP/DCAF1~~ E3 ubiquitin-protein ligase complex, ~~VprBP/~~DCAF1 ~~may function~~ as the ~~substrate recognition module within this~~ complex. ~~For example, VprBP~~/DCAF1 ~~targets NF2~~ to the E3 ~~ubiquitin-~~ligase complex ~~for~~ ubiquitination and ~~subsequent proteasome~~-~~dependent degradation~~. In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1 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. ~~In case of infection by~~ HIV-~~2 virus, it is recruited by HIV-2 Vpx in order to hijack~~ the CUL4A-RBX1-DDB1 function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. Associated with chromatin in a DDB1-~~independent and cell cycle-dependent manner, VprBP~~/~~DCAF1 is recruited~~ to ~~chromatin~~ as ~~DNA is being replicated~~ and ~~is released from chromatin before mitosis~~.<ref>PMID:17314515</ref> <ref>PMID:~~17620334~~</ref> <ref>PMID:~~17626091~~</ref> <ref>PMID:~~17630831~~</ref> <ref>PMID:~~17609381~~</ref> <ref>PMID:~~17559673~~</ref> <ref>PMID:18524771</ref> <ref>PMID:~~18606781~~</ref> <ref>PMID:~~18332868~~</ref> <ref>PMID:18464893</ref> <ref>PMID:19264781</ref> <ref>PMID:19923175</ref> <ref>PMID:~~23063525~~</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>
	<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==
-	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]	+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
	*[[VprBP\|VprBP]]		*[[VprBP\|VprBP]]
	== References ==		== References ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Civ]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Mansp~~]]	+	[[Category: Mandrillus sphinx]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Simian immunodeficiency virus]]
-	[[Category: Bishop~~, K N~~]]	+	[[Category: Bishop KN]]
-	[[Category: Boucherit~~, V C~~]]	+	[[Category: Boucherit VC]]
-	[[Category: Christodoulou, E]]	+	[[Category: Christodoulou E]]
-	[[Category: Schwefel, D]]	+	[[Category: Schwefel D]]
-	[[Category: Stoye~~, J P~~]]	+	[[Category: Stoye JP]]
-	[[Category: Taylor~~, I A~~]]	+	[[Category: Taylor IA]]
-	[[Category: Walker~~, P A]]~~	+	[[Category: Walker PA]]
-	~~[[Category: Accessory protein]]~~	+
-	~~[[Category: Proteasomal degradation]]~~	+
-	~~[[Category: Retroviral restriction factor]]~~	+
-	~~[[Category: Siv]]~~	+
-	~~[[Category: Ubiquitylation]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 07:11, 3 July 2019

OCA — Wed, 03 Jul 2019 07:11:49 GMT

←Older revision		Revision as of 07:11, 3 July 2019
Line 1:		Line 1:

	==Crystal structure of mandrill SAMHD1 (amino acid residues 1-114) bound to Vpx isolated from mandrill and human DCAF1 (amino acid residues 1058-1396)==		==Crystal structure of mandrill SAMHD1 (amino acid residues 1-114) bound to Vpx isolated from mandrill and human DCAF1 (amino acid residues 1058-1396)==
-	<StructureSection load='5aja' size='340' side='right' caption='[[5aja]], [[Resolution\|resolution]] 2.65Å' scene=''>	+	<StructureSection load='5aja' size='340' side='right'caption='[[5aja]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5aja]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AJA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5aja]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Civ Civ], [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Mansp Mansp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AJA FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
Line 22:		Line 22:
	==See Also==		==See Also==
	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]		*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]
		+	*[[VprBP\|VprBP]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Civ]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
		+	[[Category: Mansp]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Bishop, K N]]		[[Category: Bishop, K N]]

OCA at 09:52, 10 March 2017

OCA — Fri, 10 Mar 2017 09:52:37 GMT

←Older revision		Revision as of 09:52, 10 March 2017
Line 1:		Line 1:
		+
	==Crystal structure of mandrill SAMHD1 (amino acid residues 1-114) bound to Vpx isolated from mandrill and human DCAF1 (amino acid residues 1058-1396)==		==Crystal structure of mandrill SAMHD1 (amino acid residues 1-114) bound to Vpx isolated from mandrill and human DCAF1 (amino acid residues 1058-1396)==
	<StructureSection load='5aja' size='340' side='right' caption='[[5aja]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='5aja' size='340' side='right' caption='[[5aja]], [[Resolution\|resolution]] 2.65Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5aja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aja OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aja RCSB], [http://www.ebi.ac.uk/pdbsum/5aja 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=5aja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aja OCA], [http://pdbe.org/5aja PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aja RCSB], [http://www.ebi.ac.uk/pdbsum/5aja PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aja ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 5aja" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:39, 22 April 2015

OCA — Wed, 22 Apr 2015 12:39:14 GMT

←Older revision		Revision as of 12:39, 22 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of mandrill SAMHD1 (amino acid residues 1-114) bound to Vpx isolated from mandrill and human DCAF1 (amino acid residues 1058-1396)==
		+	<StructureSection load='5aja' size='340' side='right' caption='[[5aja]], [[Resolution\|resolution]] 2.65Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5aja]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AJA FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5aja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aja OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aja RCSB], [http://www.ebi.ac.uk/pdbsum/5aja PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VPRBP_HUMAN VPRBP_HUMAN]] Component of the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex, VprBP/DCAF1 may function as the substrate recognition module within this complex. For example, VprBP/DCAF1 targets NF2 to the E3 ubiquitin-ligase complex for ubiquitination and subsequent proteasome-dependent degradation. In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1 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. In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1 function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. Associated with chromatin in a DDB1-independent and cell cycle-dependent manner, VprBP/DCAF1 is recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis.<ref>PMID:17314515</ref> <ref>PMID:17620334</ref> <ref>PMID:17626091</ref> <ref>PMID:17630831</ref> <ref>PMID:17609381</ref> <ref>PMID:17559673</ref> <ref>PMID:18524771</ref> <ref>PMID:18606781</ref> <ref>PMID:18332868</ref> <ref>PMID:18464893</ref> <ref>PMID:19264781</ref> <ref>PMID:19923175</ref> <ref>PMID:23063525</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The SAMHD1 triphosphohydrolase inhibits HIV-1 infection of myeloid and resting T cells by depleting dNTPs. To overcome SAMHD1, HIV-2 and some SIVs encode either of two lineages of the accessory protein Vpx that bind the SAMHD1 N or C terminus and redirect the host cullin-4 ubiquitin ligase to target SAMHD1 for proteasomal degradation. We present the ternary complex of Vpx from SIV that infects mandrills (SIVmnd-2) with the cullin-4 substrate receptor, DCAF1, and N-terminal and SAM domains from mandrill SAMHD1. The structure reveals details of Vpx lineage-specific targeting of SAMHD1 N-terminal "degron" sequences. Comparison with Vpx from SIV that infects sooty mangabeys (SIVsmm) complexed with SAMHD1-DCAF1 identifies molecular determinants directing Vpx lineages to N- or C-terminal SAMHD1 sequences. Inspection of the Vpx-DCAF1 interface also reveals conservation of Vpx with the evolutionally related HIV-1/SIV accessory protein Vpr. These data suggest a unified model for how Vpx and Vpr exploit DCAF1 to promote viral replication.

-	~~The entry 5aja is ON HOLD until Paper Publication~~	+	Molecular Determinants for Recognition of Divergent SAMHD1 Proteins by the Lentiviral Accessory Protein Vpx.,Schwefel D, Boucherit VC, Christodoulou E, Walker PA, Stoye JP, Bishop KN, Taylor IA Cell Host Microbe. 2015 Apr 8;17(4):489-99. doi: 10.1016/j.chom.2015.03.004. PMID:25856754<ref>PMID:25856754</ref>

-	~~Authors: Schwefel~~, D.~~, Boucherit, V~~.~~C., Christodoulou, E., Walker, P.A., Stoye, J.P., Bishop, K.N., Taylor, I.A~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of mandrill SAMHD1 (amino acid residues 1~~-~~114) bound to Vpx isolated from mandrill and human DCAF1 (amino acid residues 1058-1396)~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
-	[[Category: ~~Taylor~~, ~~I.A~~]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Bishop, K N]]
		+	[[Category: Boucherit, V C]]
	[[Category: Christodoulou, E]]		[[Category: Christodoulou, E]]
-	[[Category: Walker, P.A]]
	[[Category: Schwefel, D]]		[[Category: Schwefel, D]]
-	[[Category: Stoye, J.P]]	+	[[Category: Stoye, J P]]
-	[[Category: ~~Bishop~~, ~~K.N~~]]	+	[[Category: Taylor, I A]]
-	[[Category: ~~Boucherit~~, ~~V.C~~]]	+	[[Category: Walker, P A]]
		+	[[Category: Accessory protein]]
		+	[[Category: Proteasomal degradation]]
		+	[[Category: Retroviral restriction factor]]
		+	[[Category: Siv]]
		+	[[Category: Ubiquitylation]]
		+	[[Category: Viral protein]]

OCA: Protected "5aja" [edit=sysop:move=sysop]

OCA — Wed, 04 Mar 2015 10:39:18 GMT

Protected "5aja" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:39, 4 March 2015

OCA: New page: '''Unreleased structure''' The entry 5aja is ON HOLD until Paper Publication Authors: Schwefel, D., Boucherit, V.C., Christodoulou, E., Walker, P.A., Stoye, J.P., Bishop, K.N., Taylor, ...

OCA — Wed, 04 Mar 2015 10:39:17 GMT

New page: '''Unreleased structure''' The entry 5aja is ON HOLD until Paper Publication Authors: Schwefel, D., Boucherit, V.C., Christodoulou, E., Walker, P.A., Stoye, J.P., Bishop, K.N., Taylor, ...

New page

'''Unreleased structure'''

The entry 5aja is ON HOLD until Paper Publication

Authors: Schwefel, D., Boucherit, V.C., Christodoulou, E., Walker, P.A., Stoye, J.P., Bishop, K.N., Taylor, I.A.

Description: Crystal structure of mandrill SAMHD1 (amino acid residues 1-114) bound to Vpx isolated from mandrill and human DCAF1 (amino acid residues 1058-1396)
[[Category: Unreleased Structures]]
[[Category: Taylor, I.A]]
[[Category: Christodoulou, E]]
[[Category: Walker, P.A]]
[[Category: Schwefel, D]]
[[Category: Stoye, J.P]]
[[Category: Bishop, K.N]]
[[Category: Boucherit, V.C]]