Structural highlights
Function
TOM1_HUMAN May be involved in intracellular trafficking. Probable association with membranes.
Publication Abstract from PubMed
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.
Structure of the GAT domain of the endosomal adapter protein Tom1.,Xiao S, Ellena JF, Armstrong GS, Capelluto DG Data Brief. 2016 Feb 24;7:344-8. doi: 10.1016/j.dib.2016.02.042. eCollection 2016, Jun. PMID:26977434[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xiao S, Ellena JF, Armstrong GS, Capelluto DG. Structure of the GAT domain of the endosomal adapter protein Tom1. Data Brief. 2016 Feb 24;7:344-8. doi: 10.1016/j.dib.2016.02.042. eCollection 2016, Jun. PMID:26977434 doi:http://dx.doi.org/10.1016/j.dib.2016.02.042
