@article{Nicastro_Candel_Uhl-Mecha_beta_mRNA-2017,
author = {Nicastro, Giuseppe and Candel, Adela M. and Uhl, Michael 
          and Oregioni, Alain and Hollingworth, David and Backofen, 
          Rolf and Martin, Stephen R. and Ramos, Andres},
title = {Mechanism of beta-actin {mRNA} {Recognition} by {ZBP1}},
journal = {Cell Rep},
year = {2017},
doi = {10.1016/j.celrep.2016.12.091},
volume = {18},
user = {uhlm},
pmid = {28147274},
pages = {1187-1199},
number = {5},
issn = {2211-1247},
abstract = {Zipcode binding protein 1 (ZBP1) is an oncofetal 
            RNA-binding protein that mediates the transport and local 
            translation of beta-actin mRNA by the KH3-KH4 di-domain, 
            which is essential for neuronal development. The 
            high-resolution structures of KH3-KH4 with their respective 
            target sequences show that KH4 recognizes a non-canonical 
            GGA sequence via an enlarged and dynamic hydrophobic groove, 
            whereas KH3 binding to a core CA sequence occurs with low 
            specificity. A data-informed kinetic simulation of the 
            two-step binding reaction reveals that the overall reaction 
            is driven by the second binding event and that the moderate 
            affinities of the individual interactions favor RNA looping. 
            Furthermore, the concentration of ZBP1, but not of the 
            target RNA, modulates the interaction, which explains the 
            functional significance of enhanced ZBP1 expression during 
            embryonic development.}
}