9n0w

HTLV-1 Gag capsid from immature particles

spinqualitylabelsall models 9n0w, resolution 3.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9n0w is a 3 chain structure with sequence from Human T-cell leukemia virus type I. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.44Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q82230_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] Publication Abstract from PubMed Infection with human T-cell leukemia virus type 1 (HTLV-1) can result in adult T-cell leukemia/lymphoma and HTLV-1 associated-myelopathy/tropical spastic paraparesis. The Gag polyprotein - the major structural protein - is crucial for driving virus particle assembly, with the capsid (CA) domain as the key determinant for Gag multimerization. Here, we characterize the immature CA lattice from immature virus particles by using cryo-electron microscopy and tomography (cryo-EM/ET). We report resolving the immature CA lattice to 3.4 A resolution by single particle analysis (SPA). Our reconstruction reveals that the lattice is stabilized through a trimeric NTD inter-hexamer interface and a dimeric CTD inter-hexamer interface. Further analysis by cryo-ET reveals clear heterogeneity, notably the varying lattice curvatures and the varying distances from the CA layer to the membrane. Intriguingly, inositol hexakisphosphate (IP6) is dispensable for HTLV-1 immature particle assembly and proper immature lattice formation. These observations provide deeper insights into the molecular basis of HTLV-1 immature particle morphology as well as aid in revealing therapeutic targets. High-resolution analysis of the human T-cell leukemia virus capsid protein reveals insights into immature particle morphology.,Arndt WG, Ramezani A, Talledge N, Yu G, Yang H, Chen B, Perilla JR, Zhang W, Mansky LM Nat Commun. 2025 Dec 11. doi: 10.1038/s41467-025-67129-1. PMID:41381513 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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