Structure of the GAT domain of the endosomal adapter protein Tom1
| dc.contributor.author | Xiao, Shuyan | en |
| dc.contributor.author | Ellena, Jeffrey F. | en |
| dc.contributor.author | Armstrong, Geoffrey S. | en |
| dc.contributor.author | Capelluto, Daniel G. S. | en |
| dc.contributor.department | Biological Sciences | en |
| dc.date.accessioned | 2019-06-26T14:05:05Z | en |
| dc.date.available | 2019-06-26T14:05:05Z | en |
| dc.date.issued | 2016-02-24 | en |
| dc.description.abstract | 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. | en |
| dc.description.sponsorship | This work was funded by an American Heart Association Grant-in-Aid (13GRNT16960080) and by the Thomas F. and Kate Miller Jeffress Memorial Trust (J1028) to D.G.S.C. | en |
| dc.identifier.doi | https://doi.org/10.1016/j.dib.2016.02.042 | en |
| dc.identifier.uri | http://hdl.handle.net/10919/90663 | en |
| dc.identifier.volume | 7 | en |
| dc.language.iso | en_US | en |
| dc.publisher | Elsevier | en |
| dc.rights | Creative Commons Attribution 4.0 International | en |
| dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | en |
| dc.subject | Tom1 | en |
| dc.subject | GAT domain | en |
| dc.subject | Tollip | en |
| dc.subject | Ubiquitin | en |
| dc.subject | nuclear magnetic resonance | en |
| dc.title | Structure of the GAT domain of the endosomal adapter protein Tom1 | en |
| dc.title.serial | Data in Brief | en |
| dc.type | Article - Refereed | en |