Xiao Shuyan, Ellena Jeffrey F, Armstrong Geoffrey S, Capelluto Daniel G S
Protein Signaling Domains Laboratory, Department of Biological Sciences, Biocomplexity Institute, Virginia Tech, Blacksburg, VA 24061, USA; School of Materials and Metallurgy, Inner Mongolia University of Science and Technology, PR China.
Department of Chemistry and Biochemistry, University of Virginia, Charlottesville, VA 22904, USA.
Data Brief. 2016 Feb 24;7:344-8. doi: 10.1016/j.dib.2016.02.042. eCollection 2016 Jun.
Cellular homeostasis requires correct delivery of cell-surface receptor proteins (cargo) to their target subcellular compartments. The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments. Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain's association to Tollip's Tom1-binding domain (TBD). In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain. The estimated protein structure exhibits a bundle of three helical elements. We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.
细胞内稳态需要将细胞表面受体蛋白（货物）正确递送至其目标亚细胞区室。衔接蛋白Tom1和Tollip参与内体区室中泛素化货物的分选。Tom1向内体区室的募集是由其GAT结构域与Tollip的Tom1结合结构域（TBD）的结合介导的。在这篇数据文章中，我们报道了Tom1 GAT结构域的溶液核磁共振衍生结构。估计的蛋白质结构呈现出由三个螺旋元件组成的束状结构。我们将Tom1 GAT结构与对应于Tollip TBD结合状态和泛素结合状态的结构进行了比较。
