Jeffrey F Ellena, Wen Xiong, Xiaolin Zhao, Narasimhamurthy Shanaiah, Daniel G S Capelluto
Biomolecular NMR assignments 2017 AprEfficient trafficking of ubiquitinated receptors (cargo) to endosomes requires the recruitment of adaptor proteins that exhibit ubiquitin-binding domains for recognition and transport. Tom1 is an adaptor protein that not only associates with ubiquitinated cargo but also represents a phosphoinositide effector during specific bacterial infections. This phosphoinositide-binding property is associated with its N-terminal Vps27, Hrs, STAM (VHS) domain. Despite its biological relevance, there are no resonance assignments of Tom1 VHS available that can fully characterize its molecular interactions. Here, we report the nearly complete 1H, 15N, and 13C backbone resonance assignments of the VHS domain of human Tom1.
Jeffrey F Ellena, Wen Xiong, Xiaolin Zhao, Narasimhamurthy Shanaiah, Daniel G S Capelluto. Backbone 1H, 15N, and 13C resonance assignments of the Tom1 VHS domain. Biomolecular NMR assignments. 2017 Apr;11(1):1-4
PMID: 27704363
View Full Text