Structural unity among viral origin binding proteins: Crystal structure of the nuclease domain of adeno-associated virus Rep

Alison Burgess Hickman, Donald R. Ronning, Robert M. Kotin, Fred Dyda

Research output: Contribution to journalArticlepeer-review

102 Scopus citations

Abstract

Adeno-associated virus (AAV), unique among animal viruses in its ability to integrate into a specific chromosomal location, is a promising vector for human gene therapy. AAV Replication (Rep) protein is essential for viral replication and integration, and its amino terminal domain possesses site-specific DNA binding and endonuclease activities required for replication initiation and integration. This domain displays a novel endonuclease fold and demonstrates an unexpected structural relationship to other viral origin binding proteins such as the papillomavirus E1 protein and the SV40 T antigen. The active site, located at the bottom of a positively charged cleft, is formed by the spatial convergence of a divalent metal ion and two conserved sequence motifs that define the rolling circle replication superfamily.

Original languageEnglish (US)
Pages (from-to)327-337
Number of pages11
JournalMolecular Cell
Volume10
Issue number2
DOIs
StatePublished - Aug 2002
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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