4cc9: Difference between revisions

<StructureSection load='4cc9' size='340' side='right' caption='[[4cc9]], [[Resolution|resolution]] 2.47&Aring;' scene=''>

<table><tr><td colspan='2'>[[4cc9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Civ Civ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CC9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cc9 OCA], [http://pdbe.org/4cc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cc9 RCSB], [http://www.ebi.ac.uk/pdbsum/4cc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cc9 ProSAT]</span></td></tr>

[[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> [[http://www.uniprot.org/uniprot/SAMH1_HUMAN SAMH1_HUMAN]] Putative nuclease involved in innate immune response by acting as a negative regulator of the cell-intrinsic antiviral response. May play a role in mediating proinflammatory responses to TNF-alpha signaling.<ref>PMID:18546154</ref> <ref>PMID:19525956</ref>  [[http://www.uniprot.org/uniprot/VPX_SIVSP VPX_SIVSP]] Plays a role in nuclear translocation of the viral pre-integration complex (PIC), thus is required for the virus to infect non-dividing cells. Targets specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity results in the degradation of host SAMHD1. In turn, SAMHD1 depletion allows viral replication in host myeloid cells by preventing SAMHD1-mediated hydrolysis of intracellular dNTPs necessary for reverse transcription.

[[Category: Civ]]

[[Category: Human]]

[[Category: Bishop, K N]]

[[Category: Boucherit, V C]]

[[Category: Christodoulou, E]]

[[Category: Groom, H C.T]]

[[Category: Schwefel, D]]

[[Category: Stoye, J P]]

[[Category: Taylor, I A]]

[[Category: Walker, P A]]

[[Category: Ubiquitination]]