AI Article Synopsis
- The chapter outlines how teneurins, a type of protein, evolved from bacterial precursors known as tyrosine-aspartate (YD)-repeat proteins, highlighting pioneering bioinformatic analyses.
- It explains the structural analysis of the teneurin C-terminal domain using advanced techniques like X-ray crystallography and electron microscopy, reinforcing the link to its evolutionary origins.
- Additionally, the text discusses the role of alternative splicing in increasing the diversity and functionality of teneurins, while presenting the current understanding of how their specific structures dictate their functions.
Article Abstract
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 -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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6425310 | PMC |
| http://dx.doi.org/10.3389/fnins.2019.00183 | DOI Listing |
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