Ellena Jeffrey F, Xiong Wen, Zhao Xiaolin, Shanaiah Narasimhamurthy, Capelluto Daniel G S
Biomolecular Magnetic Resonance Facility, University of Virginia, Charlottesville, VA, 22904, USA.
Protein Signaling Domains Laboratory, Department of Biological Sciences, Biocomplexity Institute and Center for Soft Matter and Biological Physics, Virginia Tech, Blacksburg, VA, 24061, USA.
Biomol NMR Assign. 2017 Apr;11(1):1-4. doi: 10.1007/s12104-016-9709-4. Epub 2016 Oct 4.
Efficient 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 H, N, and C backbone resonance assignments of the VHS domain of human Tom1.
泛素化受体（货物）有效转运至内体需要募集具有泛素结合结构域以进行识别和运输的衔接蛋白。Tom1是一种衔接蛋白，它不仅与泛素化货物相关联，而且在特定细菌感染期间代表一种磷酸肌醇效应器。这种磷酸肌醇结合特性与其N端的Vps27、Hrs、STAM（VHS）结构域相关。尽管其具有生物学相关性，但尚无可用的Tom1 VHS共振归属能完全表征其分子相互作用。在此，我们报道了人Tom1 VHS结构域几乎完整的H、N和C主链共振归属。
