bi3004268_si_006.pdf (31.09 kB)
Conformational and Dynamic Changes at the Interface Contribute to Ligand Binding by Ubiquitin
journal contribution
posted on 2012-10-16, 00:00 authored by Monica SunddUbiquitin interacts with numerous domains and motifs
in its lifetime
that vary in structure but bind the same hydrophobic patch. To identify
the structural features of ubiquitin that make it an exceptional protein–protein
interaction partner, we have studied the interaction of ubiquitin
with the signal transducing adaptor molecule-1 ubiquitin interacting
motif (UIM) using nuclear magnetic resonance. Our studies bring to
light the role of the inherent backbone flexibility of ubiquitin in
its interactions with a large array of binding partners, revealed
from the changes in Cα chemical shifts, backbone
dynamics, and hydrogen bond lengths upon UIM binding. The crystal
structures of ubiquitin complexes lend further support to our findings,
underscoring the importance of the unique and flexible hydrogen bond
network within ubiquitin and simultaneously providing insights into
the nature of the slow motions. Taken together, our studies provide
an in-depth view of the molecular changes associated with ligand recognition
by ubiquitin.