Abstract
This chapter covers the structural chemistry and the biological aspects of Rous Sarcoma Virus (RSV) retropepsin and Avian Myeloblastosis Virus (AMV) retropepsin. The RSV, identified by Peyton Rous as a tumor-causing agent in 1911, contains an RNA genome that encodes three genes required for replication. These genes, gag, pol and env, are translated to yield three large precursor polyproteins: Gag, Gag-Pol and Env. During virus maturation, Gag and Gag-Pol are cleaved into eight different mature proteins by a viral specific protease. The AMV retropepsin and RSV retropepsin differ by only two amino acid residues, and are biochemically indistinguishable. Functionally active RSV/AMV protease is a symmetric homodimer with two identical subunits of 124 amino acids each. There is one high-resolution crystal structure of the native enzyme without a substrate or a inhibitor. The active site and the substrate binding site are formed by an obvious cleft at the dimer interface.
Original language | English (US) |
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Title of host publication | Handbook of Proteolytic Enzymes, Second Edition |
Subtitle of host publication | Volume 1: Aspartic and Metallo Peptidases |
Publisher | Elsevier |
Pages | 163-166 |
Number of pages | 4 |
Volume | 1 |
ISBN (Electronic) | 9780120796113 |
ISBN (Print) | 9780124121058 |
DOIs | |
State | Published - Jan 1 2004 |
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology