作者: Sarah A. Clark , Nathan Jespersen , Clare Woodward , Elisar Barbar
DOI: 10.1016/J.FEBSLET.2015.07.032
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摘要: Abstract A wide variety of subcellular complexes are composed one or more intrinsically disordered proteins (IDPs) that multivalent, flexible, and characterized by dynamic binding diverse partner proteins. These multivalent IDP assemblies, broad functional diversity, classified here into five categories distinguished the number chains arrangement in complex. Examples each category summarized context exceptional molecular biological properties IDPs. One type – duplex scaffolds is considered detail. Its unique features include parallel alignment two chains, formation new self-associated domains, enhanced affinity for additional bivalent ligands, ubiquitous hub protein LC8. For scaffolds, dynein intermediate chain IC nucleoporin Nup159, these features, together with inherent flexibility IDPs, central to their assembly function. IDP–LC8 interaction, distributed LC8 among multiple recognition sites, described Nup159 assembly.