1H, 13C, and 15N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5) |
| |
Authors: | Aurélien Lorin Danny Létourneau Andrée Lefebvre Jean-Guy LeHoux Pierre Lavigne |
| |
Affiliation: | 1. Département de Biochimie, Faculté de médecine et des sciences de la santé, Université de Sherbrooke, Sherbrooke, QC, J1H 5N4, Canada 2. Département de Pharmacologie, Faculté de médecine et des sciences de la santé, Université de Sherbrooke, Sherbrooke, QC, J1H 5N4, Canada
|
| |
Abstract: | Steroidogenic acute regulatory (StAR)—related lipid transfer proteins possess a START (steroidogenic acute regulatory-related lipid transfer) domain. START domains are conserved protein modules involved in the non-vesicular intracellular transport of lipids and cholesterol in mammals. Fifteen mammalian proteins, divided in five subfamilies, are reported to possess a START domain. Members of the STARD4 subfamily, i.e. STARD4, 5 and 6 are essentially single START domains and are thought to be involved in the intracellular transport of cholesterol. No structure of a cholesterol-bound START domain from this family has been resolved yet. The determination of the structure of such a complex would contribute to a better understanding of the mechanism of ligand binding and transport by START domains, two unresolved aspects of their structural biology. In this context, we have undertaken the structure determination of a ligand-bound form of STARD5 by NMR. Here, we report the 1H, 13C and 15N backbone resonance assignments of the ligand-free STARD5. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|