Mapping the Binding Site of Thiopeptide Antibiotics by Proximity-Induced Covalent Capture

Proximity-induced covalent capture (PICC) has been established for the investigation of ligand binding to composite protein/oligonucleotide target complexes. The RNA-induced attachment of the thiopeptides Thiostrepton and Nosiheptide to engineered Cys mutants of the ribosomal protein L11 was highly...

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Veröffentlicht in:	Journal of the American Chemical Society 2008-04, Vol.130 (17), p.5664-5666
Hauptverfasser:	Baumann, Sascha, Schoof, Sebastian, Harkal, Surendra D, Arndt, Hans-Dieter
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Binding Sites Cysteine - genetics Electrophoresis, Polyacrylamide Gel Ligands Models, Chemical Molecular Sequence Data Mutation Oligonucleotides - chemistry Oligonucleotides - genetics Oligonucleotides - metabolism Peptides - chemistry Peptides - genetics Peptides - metabolism Protein Interaction Mapping - methods Ribosomal Proteins - chemistry Ribosomal Proteins - genetics Ribosomal Proteins - metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Sulfhydryl Compounds - chemistry Sulfhydryl Compounds - metabolism
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Zusammenfassung:	Proximity-induced covalent capture (PICC) has been established for the investigation of ligand binding to composite protein/oligonucleotide target complexes. The RNA-induced attachment of the thiopeptides Thiostrepton and Nosiheptide to engineered Cys mutants of the ribosomal protein L11 was highly position selective and allowed mapping of their binding site at amino acid resolution.
ISSN:	0002-7863 1520-5126
DOI:	10.1021/ja710608w