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Solution structure of the capsid protein from the human T-cell leukemia virus type-I.
Khorasanizadeh S; Campos-Olivas R; Summers MF; Howard Hughes Medical
December 30, 1999
J Mol Biol. 1999 Aug 13;291(2):491-505. Unique Identifier : AIDSLINE

The solution structure of the capsid protein (CA) from the human T-cell leukemia virus type one (HTLV-I), a retrovirus that causes T-cell leukemia and HTLV-I-associated myelopathy in humans, has been determined by NMR methods. The protein consists of independent N and C-terminal domains connected by a flexible linker. The domains are structurally similar to the N-terminal "core" and C-terminal "dimerization" domains, respectively, of the human immunodeficiency virus type one (HIV-1) and equine infectious anemia virus (EIAV) capsid proteins, although several important differences exist. In particular, hydrophobic residues near the major homology region are partially buried in HTLV-I CA, which is monomeric in solution, whereas analogous residues in HIV-1 and EIAV CA project from the C-terminal domain and promote dimerization. These differences in the structure and oligomerization state of the proteins appear to be related to, and possibly controlled by, the oxidation state of conserved cysteine residues, which are reduced in HTLV-I CA but form a disulfide bond in the HIV-1 and EIAV CA crystal structures. The results are consistent with an oxidative capsid assembly mechanism, in which CA oligomerization or maturation is triggered by disulfide bo nd formation as the budding virus enters the oxidizing environment of the bloodstream. Copyright 1999 Academic Press.

JOURNAL ARTICLE Amino Acid Sequence Animal Capsid/*CHEMISTRY/GENETICS/METABOLISM Cysteine/METABOLISM Horses Human HIV-1/CHEMISTRY HTLV-I/*CHEMISTRY Infectious Anemia Virus, Equine/CHEMISTRY Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Oxidation-Reduction Peptidylprolyl Isomerase/METABOLISM Recombinant Fusion Proteins/CHEMISTRY/GENETICS/METABOLISM Sequence Homology, Amino Acid Solutions Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S.

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