Resonance assignment and secondary structure of the middle MA-3 domain and complete tandem MA-3 region of the tumour suppressor protein Pdcd4.
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-3(M) and MA-3(C)), 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 (15)N, (13)C and (1)H assignments for a construct composed of the middle MA-3 domain and subsequent linker region (MA-3(M)) and backbone assignments for the entire tandem MA-3 region of Pdcd4 (Pdcd4 MA-3(M-C)). Analysis of the backbone chemical shift data obtained indicates that Pdcd4 MA-3(M) contains eight helical regions corresponding to over 74% of the protein backbone and that Pdcd4 MA-3(M-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.
Waters
Lorna C
LC
Department of Biochemistry, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester LE1 9HN, UK. lw83@le.ac.uk
Oka
Ojore
O
Muskett
Frederick W
FW
Strong
Sarah L
SL
Schmedt
Thore
T
Klempnauer
Karl-Heinz
KH
Carr
Mark D
MD
D000595:Amino Acid Sequence; D000818:Animals; D051017:Apoptosis Regulatory Proteins / Q000737:chemistry* / Q000235:genetics; D002247:Carbon Isotopes / Q000737:chemistry; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D005822:Genetic Vectors; D006859:Hydrogen / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D012984:Software
D051017:Apoptosis Regulatory Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; C498443:Pdcd4 protein, mouse; D016601:RNA-Binding Proteins; D006859:Hydrogen