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| </table> | | </table> |
| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/GAG_HTL1A GAG_HTL1A] Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome (By similarity). | | [https://www.uniprot.org/uniprot/G9BL35_9DELA G9BL35_9DELA] Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs.[ARBA:ARBA00002374] Forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.[ARBA:ARBA00037500] Matrix protein.[ARBA:ARBA00003230] The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus.[ARBA:ARBA00037194] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Human T-cell leukemia virus type 1 (HTLV-1) has an atypical immature particle morphology compared to other retroviruses. This indicates that these particles are formed in a way that is unique. Here we report the results of cryo-electron tomography (cryo-ET) studies of HTLV-1 virus-like particles (VLPs) assembled in vitro , as well as derived from cells. This work shows that HTLV-1 employs an unconventional mechanism of Gag-Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature CA tubular arrays reveals that the primary stabilizing component in HTLV-1 is CA-NTD. Mutagenesis and biophysical analysis support this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the CA-CTD. These results are the first to provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus, and this helps explain why HTLV-1 particles are morphologically distinct.
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| Unconventional stabilization of the human T-cell leukemia virus type 1 immature Gag lattice.,Obr M, Percipalle M, Chernikova D, Yang H, Thader A, Pinke G, Porley D, Mansky LM, Dick RA, Schur FK bioRxiv. 2023 Jul 24:2023.07.24.548988. doi: 10.1101/2023.07.24.548988. Preprint. PMID:37546793<ref>PMID:37546793</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8puh" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
