6S0N

A9 peptide derived from Herceptin fab binding region

Summary for 6S0N

• Entry DOI: 10.2210/pdb6s0n/pdb
• NMR Information: BMRB: 34414
• Descriptor: GLN-ASP-VAL-ASN-THR-ALA-VAL-ALA-TRP (1 entity in total)
• Functional Keywords: her2 receptor, peptide-protein interaction, saturation transfer difference, spr technique, peptide binding protein
• Biological source: Homo sapiens
• Total number of polymer chains: 1
• Total formula weight: 1003.07

Authors

De Luca, S.,Verdoliva, V.,Saviano, M.,Fattorusso, R.,Diana, D. (deposition date: 2019-06-17, release date: 2019-11-06, Last modification date: 2024-06-19)

Primary citation

De Luca, S.,Verdoliva, V.,Saviano, M.,Fattorusso, R.,Diana, D.
SPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target.
J.Pept.Sci., 26:e3231-e3231, 2020

PubMed Abstract: The binding process of A9 peptide toward HER2-DIVMP, a synthetic model of the receptor domain IV, was studied by using the surface plasmon resonance (SPR) technique, with the aim of validating it as a fast and reliable screening method for selecting peptide ligands specifically targeting a domain of their target. To investigate the structural basis of A9 binding to the model of HER2-DIVMP, multiple ligand-based nuclear magnetic resonance (NMR) methods were applied. The use of saturation transfer difference (STD) and WaterLOGSY NMR experiments identified key residues in the peptide for the receptor binding. Moreover, the bound conformation of the A9 peptide was obtained using transferred nuclear Overhauser effect spectroscopy (trNOESY) experiments. The NMR data revealed an extended binding surface that confirms an in silico model previously reported. These structural findings could provide good starting points for future lead structures optimization specific for the receptor target.

PubMed: 31749266
DOI: 10.1002/psc.3231

Experimental method

SOLUTION NMR