Tyrosine - a structural glue for hierarchical protein assembly

Trends Biochem Sci. 2024 Apr 22:S0968-0004(24)00080-X. doi: 10.1016/j.tibs.2024.03.014. Online ahead of print.ABSTRACTProtein self-assembly, guided by the interplay of sequence- and environment-dependent liquid-liquid phase separation (LLPS), constitutes a fundamental process in the assembly of numerous intrinsically disordered proteins. Heuristic examination of these proteins has underscored the role of tyrosine residues, evident in their conservation and pivotal involvement in initiating LLPS and subsequent liquid-solid phase transitions (LSPT). The development of tyrosine-templated constructs, designed to mimic their natural counterparts, emerges as a promising strategy for creating adaptive, self-assembling systems with diverse applications. This review explores the central role of tyrosine in orchestrating protein self-assembly, delving into key interactions and examining its potential in innovative applications, including responsive biomaterials and bioengineering.PMID:38653686 | DOI:10.1016/j.tibs.2024.03.014
Source: Trends in Biochemical Sciences - Category: Biochemistry Authors: Source Type: research