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8PUB

Structure of immature HTLV-1 CA-NTD from in vitro assembled MA126-CANC tubes: axis angle 0 degrees

Summary for 8PUB
Entry DOI10.2210/pdb8pub/pdb
EMDB information17929 17930 17931 17932 17933 17934 17935 17936 17937 17938 17939 17940 17941 17942 17943
DescriptorGag protein (Fragment) (1 entity in total)
Functional Keywordsretrovirus, htlv, immature capsid, ca, ca-ntd, viral protein
Biological sourceHuman T-cell leukemia virus type I
Total number of polymer chains3
Total formula weight41909.43
Authors
Obr, M.,Percipalle, M.,Chernikova, D.,Yang, H.,Thader, A.,Pinke, G.,Porley, D.,Mansky, L.M.,Dick, R.A.,Schur, F.K.M. (deposition date: 2023-07-17, release date: 2023-08-23, Last modification date: 2024-09-18)
Primary citationObr, M.,Percipalle, M.,Chernikova, D.,Yang, H.,Thader, A.,Pinke, G.,Porley, D.,Mansky, L.M.,Dick, R.A.,Schur, F.K.M.
Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice.
Nat.Struct.Mol.Biol., 2024
Cited by
PubMed Abstract: Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron tomography studies of HTLV-1 virus-like particles assembled in vitro, as well as derived from cells. This work shows that HTLV-1 uses a distinct mechanism of Gag-Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature capsid (CA) tubular arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal domain of CA. Mutagenesis analysis supports this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the C-terminal domain of CA. These results provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain why HTLV-1 particles are morphologically distinct.
PubMed: 39242978
DOI: 10.1038/s41594-024-01390-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

226707

건을2024-10-30부터공개중

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