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Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/9434

Title: Resonance assignment and secondary structure of the middle MA-3 domain and complete tandem MA-3 region of the tumour suppressor protein Pdcd4
Authors: Waters, Lorna C.
Oka, Ojore
Muskett, Frederick W.
Strong, Sarah L.
Schmedt, Thore
Klempnauer, Karl-Heinz
Carr, Mark D.
Issue Date: Apr-2010
Publisher: Springer Verlag
Citation: Biomolecular NMR Assignments, 2010, 4 (1), pp. 49-53.
Abstract: Pdcd4 (Programmed Cell Death Protein 4) is a novel eukaryotic tumour suppressor protein, which is involved in the regulation of both transcription and translation (reviewed in Lankat-Buttgereit and Göke 2009). The protein contains two interacting MA-3 domains (MA-3M and MA-3C), which are linked by a short semi-flexible linker region (Waters et al. 2007; Suzuki et al. 2008). The MA-3 domains are involved in mediating specific protein–protein interactions with functional partners such as eIF4A (Yang et al. 2003 ). Here we report essentially complete backbone and side chain 15N, 13C and 1H assignments for a construct composed of the middle MA-3 domain and subsequent linker region (MA-3M) and backbone assignments for the entire tandem MA-3 region of Pdcd4 (Pdcd4 MA-3M-C). Analysis of the backbone chemical shift data obtained indicates that Pdcd4 MA-3M contains eight helical regions corresponding to over 74% of the protein backbone and that Pdcd4 MA-3M-C contains fifteen helical regions (72%). Comparison of the position of these helical regions with those observed in the crystal structures suggests that the solution and crystal structures of both proteins are very similar.
ISSN: 1874-2718
eISSN: 1874-270X
Links: http://dx.doi.org/10.1007/s12104-009-9205-1
http://hdl.handle.net/2381/9434
http://www.springerlink.com/content/p0508m815(...)
Version: Publisher version
Status: Peer reviewed
Type: Article
Rights: Copyright © 2009 the Authors. This article is published with open access at Springerlink.com, so that the final published version can be archived in institutional repositories and can be made publicly accessible immediately. The original publication is also available at www.springerlink.com.
Appears in Collections:Published Articles, Dept. of Biochemistry

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