Difference between revisions of "Part:BBa K2356002"

Latest revision as of 10:18, 27 October 2017

14-3-3 dimer

Proteins belonging to the 14-3-3 family are dimers, where each monomer consists out of nine anti-parallel α-helices. This causes the dimer to obtain a cup-like shape with two amphipathic binding grooves. The structure forms a rigid scaffold that is capable of anchoring proteins. 14-3-3 proteins are involved in multiple cellular processes and are mostly known to bind phosphorylated peptide motifs, especially those containing phosphoserine and phosphothreonine sequences. Most regions are conserved among different 14-3-3 isoforms, but the C-terminus appears to show more variability and is important in binding different target proteins.[1]

In this project, the specific tobacco isoform 14-3-3c is used and stripped of its last 18 C-terminal amino acids, called T14-3cΔC. This allows higher affinity towards the CT52 peptide, more specifically the YDI tail (see Figure 1), in the presence of small molecule fusicoccin.[2]

The protein mass is 60 kDa.

[1] Obsilova V, Kopecka M, Kosek D, Kacirova M, Kylarova S. Mechanisms of the 14-3-3 Protein Function : Regulation of Protein Function Through Conformational Modulation. 2014;63. [2] Ottmann C, Marco S, Jaspert N, et al. Article Structure of a 14-3-3 Coordinated Hexamer of the Plant Plasma Membrane H + -ATPase by Combining X-Ray Crystallography and Electron Cryomicroscopy. 2007:427-440. doi:10.1016/j.molcel.2006.12.017.

Sequence and Features