1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex.
EH domains are protein-protein interaction domains that function in vesicular trafficking and endocytosis. 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.
Rumpf
Julia
J
Department of Biomolecular Mechanisms, Max-Planck-Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. julia.rumpf@mpimf-heidelberg.mpg.de
Simon
Bernd
B
Groemping
Yvonne
Y
Sattler
Michael
M
D033942:Adaptor Proteins, Vesicular Transport / Q000737:chemistry*; D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D046912:Multiprotein Complexes / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D011522:Protons; D033921:Vesicular Transport Proteins / Q000737:chemistry*
D033942:Adaptor Proteins, Vesicular Transport; D002247:Carbon Isotopes; C486204:EPN2 protein, human; D046912:Multiprotein Complexes; D009587:Nitrogen Isotopes; D011522:Protons; C429267:STON2 protein, human; D033921:Vesicular Transport Proteins