Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid.

ABSTRACT: Twenty-eight amino acid residues involved in most noncovalent interactions between trimeric protein subunits in the capsid of the parvovirus minute virus of mice were truncated individually to alanine, and the effects on capsid assembly, thermostability, and conformation were analyzed. Only seven side chains were essential for protein subunit recognition. These side chains virtually corresponded with those that either buried a large hydrophobic surface on trimer association or formed buried intertrimer hydrogen bonds or salt bridges. The seven residues are evolutionarily conserved, and they define regularly spaced spots on a thin equatorial belt surrounding each trimer. Truncation of the many side chains that were dispensable for assembly, including those participating in solvent-accessibl

SUBMITTER: Reguera J 

PROVIDER: S-EPMC365688 | biostudies-literature | 2004 Mar

REPOSITORIES: biostudies-literature