7lga
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==PEG10 CA-like C-terminal domain== | |
+ | <StructureSection load='7lga' size='340' side='right'caption='[[7lga]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
+ | == 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> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | ||
+ | <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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 7lga" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Ganser-Pornillos BK]] | ||
+ | [[Category: Pornillos O]] | ||
+ | [[Category: Zurowska K]] |
Current revision
PEG10 CA-like C-terminal domain
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