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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-08DB-2 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-DE2D-5
Genre: Journal Article

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BiomolNMRAssign_2_2008_55.pdf (Any fulltext), 492KB
 
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https://dx.doi.org/10.1007/s12104-008-9083-y (Any fulltext)
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 Creators:
Rumpf, Julia1, Author           
Simon, Bernd, Author
Groemping, Yvonne1, Author           
Sattler, Michael, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: EH domains − Eps15 − Stonin 2 − Protein-protein interactions − Endocytosis
 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

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Language(s): eng - English
 Dates: 2007-12-122008-03-142008-03-292008-06-01
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s12104-008-9083-y
URI: http://www.ncbi.nlm.nih.gov/pubmed/19636924
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Title: Biomolecular NMR assignments
  Abbreviation : J. Biomol. NMR
Source Genre: Journal
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Publ. Info: Dordrecht, The Netherlands : Springer
Pages: - Volume / Issue: 2 (1) Sequence Number: - Start / End Page: 55 - 58 Identifier: ISSN: 1874-2718