Photochemically-Activated Probes of Protein−Protein Interactions
| Autor: | Richard S. Agnes, David S. Lawrence, Sandip K. Nandy |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Time Factors Light Photochemistry Peptide Plasma protein binding SH2 domain Sensitivity and Specificity Biochemistry Article Protein–protein interaction src Homology Domains Structure-Activity Relationship Structure–activity relationship Moiety Phosphorylation Physical and Theoretical Chemistry Binding site chemistry.chemical_classification Binding Sites Molecular Structure biology Chemistry Organic Chemistry Active site Cyclic AMP-Dependent Protein Kinases biology.protein Biophysics Oligonucleotide Probes Peptide Hydrolases Protein Binding |
| Zdroj: | Organic Letters. 9:2249-2252 |
| ISSN: | 1523-7052 1523-7060 |
| DOI: | 10.1021/ol070238t |
| Popis: | The activity of light-activatable ("caged") compounds can be temporally and spatially controlled, thereby providing a means to interrogate intracellular biochemical pathways as a function of time and space. Nearly all caged peptides contain photocleavable groups positioned on the side chains of key residues. We describe an alternative active site targeted strategy that disrupts the interaction between the protein target (SH2 domain, kinase, and proteinase) and a critical amide NH moiety of the peptide probe. |
| Databáze: | OpenAIRE |
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