AI Article Synopsis
- Understanding tau polymerization is crucial for developing ways to inhibit the formation of harmful structures associated with neurodegenerative diseases.
- The tau protein has a microtubule-binding domain with key hexapeptide sequences that play a significant role in its polymerization process.
- This study reveals that a specific interaction between amino acids Ile308 and Tyr310 is vital for establishing a unique "steric zipper" structure in tau amyloid fibrils.
Article Abstract
Investigation of the mechanism of tau polymerization is indispensable for finding inhibitory conditions or identifying compounds preventing the formation of paired helical filament or oligomers. Tau contains a microtubule-binding domain consisting of three or four repeats in its C-terminal half. It has been considered that the key event in tau polymerization is the formation of a β-sheet structure arising from a short hexapeptide (306)VQIVYK(311) in the third repeat of tau. In this paper, we report for the first time that the C-H⋯π interaction between Ile308 and Tyr310 is the elemental structural scaffold essential for forming a dry "steric zipper" structure in tau amyloid fibrils.
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| http://dx.doi.org/10.1016/j.febslet.2010.09.012 | DOI Listing |
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