2LOH
Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment
Summary for 2LOH
| Entry DOI | 10.2210/pdb2loh/pdb |
| Related | 2LLM |
| Descriptor | P3(42) (1 entity in total) |
| Functional Keywords | neuropeptide |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: P05067 |
| Total number of polymer chains | 2 |
| Total formula weight | 8900.92 |
| Authors | Nadezhdin, K.,Bocharov, E.,Bocharova, O.,Arseniev, A. (deposition date: 2012-01-24, release date: 2012-05-23, Last modification date: 2024-05-15) |
| Primary citation | Nadezhdin, K.D.,Bocharova, O.V.,Bocharov, E.V.,Arseniev, A.S. Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment. Febs Lett., 586:1687-1692, 2012 Cited by PubMed Abstract: Some pathogenic mutations associated with Alzheimer's disease are thought to affect structural-dynamic properties and the lateral dimerization of amyloid precursor protein (APP) in neuron membrane. Dimeric structure of APP transmembrane fragment Gln(686)-Lys(726) was determined in membrane-mimicking dodecylphosphocholine micelles using high-resolution NMR spectroscopy. The APP membrane-spanning α-helix Lys(699)-Lys(724) self-associates in a left-handed parallel dimer through extended heptad repeat motif I(702)X(3)M(706)X(2)G(709)X(3)A(713)X(2)I(716)X(3)I(720)X(2)I(723), whereas the juxtamembrane region Gln(686)-Val(695) constitutes the nascent helix, also sensing the dimerization. The dimerization mechanism of APP transmembrane domain has been described at atomic resolution for the first time and is important for understanding molecular events of APP sequential proteolytical cleavage resulting in amyloid-β peptide. PubMed: 22584060DOI: 10.1016/j.febslet.2012.04.062 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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