Teneurin Structures Are Composed of Ancient Bacterial Protein Domains.
| Autor: | Jackson VA; MRC Laboratory of Molecular Biology, Cambridge, United Kingdom., Busby JN; School of Biological Sciences, The University of Auckland, Auckland, New Zealand., Janssen BJC; Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Faculty of Science, Utrecht University, Utrecht, Netherlands., Lott JS; School of Biological Sciences, The University of Auckland, Auckland, New Zealand., Seiradake E; Department of Biochemistry, University of Oxford, Oxford, United Kingdom. |
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| Jazyk: | angličtina |
| Zdroj: | Frontiers in neuroscience [Front Neurosci] 2019 Mar 13; Vol. 13, pp. 183. Date of Electronic Publication: 2019 Mar 13 (Print Publication: 2019). |
| DOI: | 10.3389/fnins.2019.00183 |
| Abstrakt: | Pioneering bioinformatic analysis using sequence data revealed that teneurins evolved from bacterial tyrosine-aspartate (YD)-repeat protein precursors. Here, we discuss how structures of the C-terminal domain of teneurins, determined using X -ray crystallography and electron microscopy, support the earlier findings on the proteins' ancestry. This chapter describes the structure of the teneurin scaffold with reference to a large family of teneurin-like proteins that are widespread in modern prokaryotes. The central scaffold of modern eukaryotic teneurins is decorated by additional domains typically found in bacteria, which are re-purposed in eukaryotes to generate highly multifunctional receptors. We discuss how alternative splicing contributed to further diversifying teneurin structure and thereby function. This chapter traces the evolution of teneurins from a structural point of view and presents the state-of-the-art of how teneurin function is encoded by its specific structural features. |
| Databáze: | MEDLINE |
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