BCL-2 Protein Family Interaction Analysis by Nuclear Magnetic Resonance Spectroscopy

Methods Mol Biol. 2019:1877:217-231. doi: 10.1007/978-1-4939-8861-7_15.

Abstract

Biomolecular nuclear magnetic resonance (NMR) is a powerful and versatile method for studying both protein-protein interactions (PPIs) and protein-small molecule binding. NMR has been used extensively in the investigation of BCL-2 family proteins revealing the structure of key family members, identifying binding partners and interaction sites, and screening small molecule modulators. In this chapter we discuss the application of NMR to identify interaction sites and structure determination of protein-protein and protein-small molecule complexes using two examples.

Keywords: BAX; BCL-2; BCL-2 family; Chemical shift perturbation (CSP); MCL-1; Nuclear magnetic resonance (NMR); Paramagnetic relaxation enhancement (PRE); Protein–protein interactions (PPI).

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites / physiology
  • Cell Line
  • Humans
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Protein Binding / physiology
  • Protein Interaction Domains and Motifs / physiology
  • Proto-Oncogene Proteins c-bcl-2 / metabolism*
  • Small Molecule Libraries / metabolism

Substances

  • Proto-Oncogene Proteins c-bcl-2
  • Small Molecule Libraries