Inhibition of Escherichia coli RecA by rationally redesigned N-terminal helix

Autor:	Scott F. Singleton, Daniel J. Cline, Shannon L. Holt
Rok vydání:	2007
Předmět:	Polymers Protein Conformation Chemistry Pharmaceutical Molecular Sequence Data DNA Single-Stranded Peptide medicine.disease_cause Models Biological Biochemistry Protein Structure Secondary Protein filament Inhibitory Concentration 50 chemistry.chemical_compound Adenosine Triphosphate Protein structure Escherichia coli medicine Amino Acid Sequence Enzyme Inhibitors Physical and Theoretical Chemistry Peptide sequence Adenosine Triphosphatases chemistry.chemical_classification Organic Chemistry biochemical phenomena metabolism and nutrition Molecular biology Protein Structure Tertiary Rec A Recombinases chemistry Helix Biophysics bacteria DNA Antibiotic resistance genes
Zdroj:	Organic & Biomolecular Chemistry. 5:1525
ISSN:	1477-0539 1477-0520
DOI:	10.1039/b703159a
Popis:	Bacterial RecA promotes the development and transmission of antibiotic resistance genes by self-assembling into an ATP-hydrolyzing filamentous homopolymer on single-stranded DNA. We report the design of a 29mer peptide based on the RecA N-terminal domain involved in intermonomer contact that inhibits RecA filament assembly with an IC50 of 3 microM.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c8c97d6a47750a4981e1b0c0c4cd3fb https://doi.org/10.1039/b703159a Zobrazit plný text záznamu