5vku
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==An atomic structure of the human cytomegalovirus (HCMV) capsid with its securing layer of pp150 tegument protein== | |
| + | <SX load='5vku' size='340' side='right' viewer='molstar' caption='[[5vku]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vku]] is a 62 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_AD169 Human herpesvirus 5 strain AD169]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VKU FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</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=5vku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vku OCA], [https://pdbe.org/5vku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vku RCSB], [https://www.ebi.ac.uk/pdbsum/5vku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vku ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PP150_HCMVA PP150_HCMVA] Participates in the last steps of viral maturation and release. Associates with nuclear capsids prior to DNA encapsidation and later preserves the integrity of nucleocapsids through secondary envelopment at the assembly compartment. Interacts with host CCNA2 and thereby blocks the onset of lytic gene expression to promote establishment of a quiescent state of infection in undifferentiated cells.<ref>PMID:16873276</ref> <ref>PMID:18653449</ref> <ref>PMID:21411515</ref> <ref>PMID:23966856</ref> <ref>PMID:24101496</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Herpesviruses possess a genome-pressurized capsid. The 235-kilobase genome of human cytomegalovirus (HCMV) is by far the largest of any herpesvirus, yet it has been unclear how its capsid, which is similar in size to those of other herpesviruses, is stabilized. Here we report a HCMV atomic structure consisting of the herpesvirus-conserved capsid proteins MCP, Tri1, Tri2, and SCP and the HCMV-specific tegument protein pp150-totaling ~4000 molecules and 62 different conformers. MCPs manifest as a complex of insertions around a bacteriophage HK97 gp5-like domain, which gives rise to three classes of capsid floor-defining interactions; triplexes, composed of two "embracing" Tri2 conformers and a "third-wheeling" Tri1, fasten the capsid floor. HCMV-specific strategies include using hexon channels to accommodate the genome and pp150 helix bundles to secure the capsid via cysteine tetrad-to-SCP interactions. Our structure should inform rational design of countermeasures against HCMV, other herpesviruses, and even HIV/AIDS. | ||
| - | + | Atomic structure of the human cytomegalovirus capsid with its securing tegument layer of pp150.,Yu X, Jih J, Jiang J, Zhou ZH Science. 2017 Jun 30;356(6345). pii: eaam6892. doi: 10.1126/science.aam6892. PMID:28663444<ref>PMID:28663444</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5vku" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Human herpesvirus 5 strain AD169]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jiang J]] | ||
| + | [[Category: Jih J]] | ||
| + | [[Category: Yu X]] | ||
| + | [[Category: Zhou H]] | ||
Current revision
An atomic structure of the human cytomegalovirus (HCMV) capsid with its securing layer of pp150 tegument protein
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