|Title||Structural Characterization of the Self-Association Domain of Swallow.|
|Publication Type||Journal Article|
|Year of Publication||2021|
|Authors||Loening NM, Barbar E|
|Date Published||2021 Feb 27|
Swallow, a 62 kDa multidomain protein, is required for the proper localization of several mRNAs involved in the development of Drosophila oocytes. The dimerization of Swallow depends on a 71-residue self-association domain in the center of the protein sequence, and is significantly stabilized by a binding interaction with dynein light chain (LC8). Here, we detail the use of solution-state nuclear magnetic resonance (NMR) spectroscopy to characterize the structure of this self-association domain, thereby establishing that this domain forms a parallel coiled-coil and providing insight into how the stability of the dimerization interaction is regulated. This article is protected by copyright. All rights reserved.
|Alternate Journal||Protein Sci|