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  A combination of spin diffusion methods for the determination of protein-ligand complex structural ensembles.

Pilger, J., Mazur, A., Monecke, P., Schreuder, H., Elshorst, B., Bartoschek, S., et al. (2015). A combination of spin diffusion methods for the determination of protein-ligand complex structural ensembles. Angewandte Chemie International Edition, 54(22), 6511-6515. doi:10.1002/anie.201500671.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-C6DA-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-D58F-1
Genre: Journal Article

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 Creators:
Pilger, J.1, Author              
Mazur, A.1, Author              
Monecke, P., Author
Schreuder, H., Author
Elshorst, B., Author
Bartoschek, S., Author
Langer, T, Author
Schiffer, A., Author
Krimm, I., Author
Wegstroht, M.1, Author              
Lee, D.1, Author              
Hessler, G., Author
Wendt, K. U., Author
Becker, S.1, Author              
Griesinger, C.1, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: NMR spectroscopy; drug design; glycogen phosphorylase; kinases; soluble epoxide hydrolase
 Abstract: Structure-based drug design (SBDD) is a powerful and widely used approach to optimize affinity of drug candidates. With the recently introduced INPHARMA method, the binding mode of small molecules to their protein target can be characterized even if no spectroscopic information about the protein is known. Here, we show that the combination of the spin-diffusion-based NMR methods INPHARMA, trNOE, and STD results in an accurate scoring function for docking modes and therefore determination of protein-ligand complex structures. Applications are shown on the model system protein kinase A and the drug targets glycogen phosphorylase and soluble epoxide hydrolase (sEH). Multiplexing of several ligands improves the reliability of the scoring function further. The new score allows in the case of sEH detecting two binding modes of the ligand in its binding site, which was corroborated by X-ray analysis.

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Language(s): eng - English
 Dates: 2015-04-152015-05-26
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201500671
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 54 (22) Sequence Number: - Start / End Page: 6511 - 6515 Identifier: -