Mechanistic studies of affinity modulation

M. K. Rosen, C. D. Amos, T. J. Wandless

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)11979-11982
Number of pages4
JournalJournal of the American Chemical Society
Volume122
Issue number48
DOIs
StatePublished - Dec 6 2000

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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