7p70

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7p70]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_papillomavirus_35 Human papillomavirus 35]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P70 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7p70]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_papillomavirus_35 Human papillomavirus 35]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P70 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7p70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p70 OCA], [https://pdbe.org/7p70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p70 RCSB], [https://www.ebi.ac.uk/pdbsum/7p70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p70 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=7p70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p70 OCA], [https://pdbe.org/7p70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p70 RCSB], [https://www.ebi.ac.uk/pdbsum/7p70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p70 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/VE6_HPV35 VE6_HPV35] This protein may be involved in the oncogenic potential of this virus (associated with cancer of the uterine cervix). Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.[HAMAP-Rule:MF_04006]
[https://www.uniprot.org/uniprot/VE6_HPV35 VE6_HPV35] This protein may be involved in the oncogenic potential of this virus (associated with cancer of the uterine cervix). Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.[HAMAP-Rule:MF_04006]
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==See Also==
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*[[Syntrophin|Syntrophin]]
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</StructureSection>
</StructureSection>

Current revision

The PDZ-domain of SNTB1 complexed with the PDZ-binding motif of HPV35-E6

PDB ID 7p70

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