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Journal Article

1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex

MPS-Authors
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Rumpf,  Julia
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Groemping,  Yvonne
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://link.springer.com/content/pdf/10.1007%2Fs12104-008-9083-y.pdf
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https://dx.doi.org/10.1007/s12104-008-9083-y
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Citation

Rumpf, J., Simon, B., Groemping, Y., & Sattler, M. (2008). 1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex. Biomolecular NMR assignments, 2(1), 55-58. doi:10.1007/s12104-008-9083-y.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-08DB-2
Abstract
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