Document 0778
 DOCN  M9590778
 TI    A molecular determinant of human immunodeficiency virus particle
       assembly located in matrix antigen p17.
 DT    9509
 AU    Morikawa Y; Kishi T; Zhang WH; Nermut MV; Hockley DJ; Jones IM; Kitasato
       Institute, Kitasato University, Tokyo, Japan.
 SO    J Virol. 1995 Jul;69(7):4519-23. Unique Identifier : AIDSLINE
       MED/95287512
 AB    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.
 DE    Base Sequence  Gene Products, gag/*CHEMISTRY  HIV-1/*CHEMISTRY
       Molecular Sequence Data  Point Mutation  Protein Precursors/*CHEMISTRY
       Protein Structure, Secondary  Structure-Activity Relationship  Support,
       Non-U.S. Gov't  Virion/*CHEMISTRY  JOURNAL ARTICLE

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