Backbone 1H, 15N,and 13C resonance assignments of the Tom1 VHS domain |
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| Authors: | Jeffrey F. Ellena Wen Xiong Xiaolin Zhao Narasimhamurthy Shanaiah Daniel G. S. Capelluto |
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| Affiliation: | 1.Biomolecular Magnetic Resonance Facility,University of Virginia,Charlottesville,USA;2.Protein Signaling Domains Laboratory, Department of Biological Sciences, Biocomplexity Institute and Center for Soft Matter and Biological Physics,Virginia Tech,Blacksburg,USA;3.Department of Chemistry,Virginia Tech,Blacksburg,USA |
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| Abstract: | 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 1H, 15N, and 13C backbone resonance assignments of the VHS domain of human Tom1. |
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