Mechanistic studies of affinity modulation Journal Article
| Authors: | Rosen, M. K.; Amos, C. D.; Wandless, T. J. |
| Article Title: | Mechanistic studies of affinity modulation |
| Abstract: | A synthetic ligand for the protein FKBP12 was covalently linked to a peptide ligand (pYEEI) for the Fyn SH2 protein to create a bifunctional molecule called SLFpYEEI. This bifunctional molecule can simultaneously bind both proteins to form a trimeric complex. When SLFpYEEI is precomplexed with FKBP12, the peptide ligand binds 6-fold more weakly to the Fyn SH2 domain than SLFpYEEI alone. Isotope-edited NMR spectroscopy was used to investigate the molecular basis for the observed reduction in affinity. The results suggest that interactions between the pYEEI peptide and FKBP12 may play a significant role in diminishing the affinity of SLFpYEEI for the Fyn SH2 domain. |
| Keywords: | binding affinity; protein domain; complex formation; protein protein interaction; protein binding; protein tyrosine kinase; ligand; ligand binding; article |
| Journal Title: | Journal of the American Chemical Society |
| Volume: | 122 |
| Issue: | 48 |
| ISSN: | 0002-7863 |
| Publisher: | American Chemical Society |
| Date Published: | 2000-12-06 |
| Start Page: | 11979 |
| End Page: | 11982 |
| Language: | English |
| DOI: | 10.1021/ja002991m |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 18 November 2015 -- Source: Scopus |
