| Autor: |
Morikawa, Y, Kishi, T, Zhang, W H, Nermut, M V, Hockley, D J, Jones, I M |
| Zdroj: |
The Journal of Virology; July 1995, Vol. 69 Issue: 7 p4519-4523, 5p |
| Abstrakt: |
We report single-point mutations that are located in the matrix protein domain of the gag gene of human immunodeficiency virus type 1 and that prevent Gag particle formation. We show that mutations of p17 that abolish human immunodeficiency virus particle assembly also prevent the dimerization of p17 protein, as measured directly by a protein-protein binding assay. In the three-dimensional structure of p17, mutations that abolish dimerization are located in a single alpha helix that forms part of a fingerlike projection from one side of the molecule. Peptides derived from this region of p17 also reduce the level of p17 dimer when they are added to p17-expressing cells and compete for p17 self-association when present in protein-protein binding assays. We propose that the dimerization of the Gag precursor that occurs by the interdigitation of alpha helices on adjacent matrix molecules is a key stage in virion assembly and that the prevention of such an interaction is the molecular basis of particle misassembly. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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