t140-peptide and 4-azidophenylalanine

t140-peptide has been researched along with 4-azidophenylalanine* in 1 studies

Other Studies

1 other study(ies) available for t140-peptide and 4-azidophenylalanine

Article	Year
Mapping the ligand-binding site on a G protein-coupled receptor (GPCR) using genetically encoded photocrosslinkers. Biochemistry, 2011, May-03, Volume: 50, Issue:17 We developed a general cell-based photocrosslinking approach to investigate the binding interfaces necessary for the formation of G protein-coupled receptor (GPCR) signaling complexes. The two photoactivatable unnatural amino acids p-benzoyl-L-phenylalanine and p-azido-L-phenylalanine were incorporated by amber codon suppression technology into CXC chemokine receptor 4 (CXCR4). We then probed the ligand-binding site for the HIV-1 coreceptor blocker, T140, using a fluorescein-labeled T140 analogue. Among eight amino acid positions tested, we found a unique UV-light-dependent crosslink specifically between residue 189 and T140. These results are evaluated with molecular modeling using the crystal structure of CXCR4 bound to CVX15. Topics: Azides; Benzophenones; Binding Sites; Cross-Linking Reagents; Fluoresceins; Fluorescent Dyes; HEK293 Cells; HIV-1; Humans; Ligands; Models, Molecular; Mutation; Oligopeptides; Phenylalanine; Protein Binding; Receptors, CXCR4; Ultraviolet Rays	2011

Article

Year

Mapping the ligand-binding site on a G protein-coupled receptor (GPCR) using genetically encoded photocrosslinkers.

Biochemistry, 2011, May-03, Volume: 50, Issue:17

We developed a general cell-based photocrosslinking approach to investigate the binding interfaces necessary for the formation of G protein-coupled receptor (GPCR) signaling complexes. The two photoactivatable unnatural amino acids p-benzoyl-L-phenylalanine and p-azido-L-phenylalanine were incorporated by amber codon suppression technology into CXC chemokine receptor 4 (CXCR4). We then probed the ligand-binding site for the HIV-1 coreceptor blocker, T140, using a fluorescein-labeled T140 analogue. Among eight amino acid positions tested, we found a unique UV-light-dependent crosslink specifically between residue 189 and T140. These results are evaluated with molecular modeling using the crystal structure of CXCR4 bound to CVX15.

Topics: Azides; Benzophenones; Binding Sites; Cross-Linking Reagents; Fluoresceins; Fluorescent Dyes; HEK293 Cells; HIV-1; Humans; Ligands; Models, Molecular; Mutation; Oligopeptides; Phenylalanine; Protein Binding; Receptors, CXCR4; Ultraviolet Rays

2011