Title | Structural Characterization of the Self-Association Domain of Swallow. |
Publication Type | Journal Article |
Year of Publication | 2021 |
Authors | Loening NM, Barbar E |
Journal | Protein Sci |
Date Published | 2021 Feb 27 |
ISSN | 1469-896X |
Abstract | 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. |
DOI | 10.1002/pro.4055 |
Alternate Journal | Protein Sci |
PubMed ID | 33641207 |