~1H, ~(13)C, and ~(15)N chemical shift assignments for the Epsl5-EH2-stonin 2 complex

摘要

EH domains are protein-protein interaction domains that function in vesicular trafficking and endo-cytosis. Here, we report the NMR spectral assignments of the high-affinity complex between the second EH domain of Eps15 and a stonin 2 peptide—providing the basis for the characterization of a two-site binding mode. Eps15 has been implicated in clathrin-mediated endo-cytosis as an assembly factor for the endocytic protein machinery (Salcini et al. 1999). Its N-terminus comprises three Eps15 homology (EH) domains, protein interaction modules that are exclusively found in proteins involved in vesicular trafficking.