7lga
From Proteopedia
(Difference between revisions)
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==PEG10 CA-like C-terminal domain== | ==PEG10 CA-like C-terminal domain== | ||
| - | <StructureSection load='7lga' size='340' side='right'caption='[[7lga]]' scene=''> | + | <StructureSection load='7lga' size='340' side='right'caption='[[7lga]], [[Resolution|resolution]] 1.90Å' 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=7LGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7lga]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGA 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=7lga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lga OCA], [https://pdbe.org/7lga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lga RCSB], [https://www.ebi.ac.uk/pdbsum/7lga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lga ProSAT]</span></td></tr> | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7lga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lga OCA], [https://pdbe.org/7lga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lga RCSB], [https://www.ebi.ac.uk/pdbsum/7lga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lga ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/PEG10_HUMAN PEG10_HUMAN]] Prevents apoptosis in hepatocellular carcinoma (HCC) cells through interaction with SIAH1, a mediator of apoptosis (PubMed:12810624). May also have a role in cell growth promotion and hepatoma formation (PubMed:12810624, PubMed:16423995). Inhibits the TGF-beta signaling by interacting with the TGF-beta receptor ACVRL1 (PubMed:15611116). When overexpressed, induces the formation of cellular extension, such as filipodia in association with ACVRL1 (PubMed:15611116). Involved at the immediate early stage of adipocyte differentiation (By similarity). May bind to the 5'-GCCTGTCTTT-3' DNA sequence of the MB1 domain in the myelin basic protein (MBP) promoter (By similarity).[UniProtKB:Q7TN75]<ref>PMID:12810624</ref> <ref>PMID:15611116</ref> <ref>PMID:16423995</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Gag proteins of retroviruses play an essential role in virus particle assembly by forming a protein shell or capsid and thus generating the virion compartment. A variety of human proteins have now been identified with structural similarity to one or more of the major Gag domains. These human proteins are thought to have been evolved or "domesticated" from ancient integrations due to retroviral infections or retrotransposons. Here, we report that X-ray crystal structures of stably folded domains of MOAP1 (modulator of apoptosis 1) and PEG10 (paternally expressed gene 10) are highly similar to the C-terminal capsid (CA) domains of cognate Gag proteins. The structures confirm classification of MOAP1 and PEG10 as domesticated Gags, and suggest that these proteins may have preserved some of the key interactions that facilitated assembly of their ancestral Gags into capsids. | ||
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| + | Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins.,Zurowska K, Alam A, Ganser-Pornillos BK, Pornillos O Proteins. 2021 Aug 6. doi: 10.1002/prot.26204. PMID:34357660<ref>PMID:34357660</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7lga" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ganser-Pornillos | + | [[Category: Ganser-Pornillos, B K]] |
| - | [[Category: Pornillos O]] | + | [[Category: Pornillos, O]] |
| - | [[Category: Zurowska K]] | + | [[Category: Zurowska, K]] |
| + | [[Category: Domesticated gag]] | ||
| + | [[Category: Imprinted gene]] | ||
| + | [[Category: Oncoprotein]] | ||
Revision as of 14:16, 29 December 2021
PEG10 CA-like C-terminal domain
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