2N7Q
Structure of the transmembrane domain of human nicastrin in SDS micelles
Summary for 2N7Q
| Entry DOI | 10.2210/pdb2n7q/pdb |
| Related | 2N7R |
| NMR Information | BMRB: 25817 |
| Descriptor | Nicastrin (1 entity in total) |
| Functional Keywords | detergent micelles, gamma-secretase, nicastrin, membrane protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane ; Single-pass type I membrane protein : Q92542 |
| Total number of polymer chains | 1 |
| Total formula weight | 5992.00 |
| Authors | |
| Primary citation | Li, Y.,Liew, L.S.,Li, Q.,Kang, C. Structure of the transmembrane domain of human nicastrin-a component of gamma-secretase Sci Rep, 6:19522-19522, 2016 Cited by PubMed Abstract: Nicastrin is the largest component of γ-secretase that is an intramembrane protease important in the development of Alzheimer's disease. Nicastrin contains a large extracellular domain, a single transmembrane (TM) domain, and a short C-terminus. Its TM domain is important for the γ-secretase complex formation. Here we report nuclear magnetic resonance (NMR) studies of the TM and C-terminal regions of human nicastrin in both sodium dodecyl sulfate (SDS) and dodecylphosphocholine (DPC) micelles. Structural study and dynamic analysis reveal that the TM domain is largely helical and stable under both SDS and DPC micelles with its N-terminal region undergoing intermediate time scale motion. The TM helix contains a hydrophilic patch that is important for TM-TM interactions. The short C-terminus is not structured in solution and a region formed by residues V697-A702 interacts with the membrane, suggesting that these residues may play a role in the γ-secretase complex formation. Our study provides structural insight into the function of the nicastrin TM domain and the C-terminus in γ-secretase complex. PubMed: 26776682DOI: 10.1038/srep19522 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
