Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural and functional mechanisms of anti-NMDAR autoimmune encephalitis.
Journal, issue, pages	Nat Struct Mol Biol, Year 2024
Publish date	Sep 3, 2024
Authors	Kevin Michalski / Taha Abdulla / Sam Kleeman / Lars Schmidl / Ricardo Gómez / Noriko Simorowski / Francesca Vallese / Harald Prüss / Manfred Heckmann / Christian Geis / Hiro Furukawa /
PubMed Abstract	Autoantibodies against neuronal membrane proteins can manifest in autoimmune encephalitis, inducing seizures, cognitive dysfunction and psychosis. Anti-N-methyl-D-aspartate receptor (NMDAR) ...Autoantibodies against neuronal membrane proteins can manifest in autoimmune encephalitis, inducing seizures, cognitive dysfunction and psychosis. Anti-N-methyl-D-aspartate receptor (NMDAR) encephalitis is the most dominant autoimmune encephalitis; however, insights into how autoantibodies recognize and alter receptor functions remain limited. Here we determined structures of human and rat NMDARs bound to three distinct patient-derived antibodies using single-particle electron cryo-microscopy. These antibodies bind different regions within the amino-terminal domain of the GluN1 subunit. Through electrophysiology, we show that all three autoantibodies acutely and directly reduced NMDAR channel functions in primary neurons. Antibodies show different stoichiometry of binding and antibody-receptor complex formation, which in one antibody, 003-102, also results in reduced synaptic localization of NMDARs. These studies demonstrate mechanisms of diverse epitope recognition and direct channel regulation of anti-NMDAR autoantibodies underlying autoimmune encephalitis.
External links	Nat Struct Mol Biol / PubMed:39227719
Methods	EM (single particle)
Resolution	3.69 - 4.42 Å
Structure data	43530 8vuh EMDB-43530, PDB-8vuh: Human GluN1-2A IgG 003-102 splayed conformation Method: EM (single particle) / Resolution: 4.42 Å 43531 8vuj EMDB-43531, PDB-8vuj: Human GluN1-2A with Fab 003-102 Method: EM (single particle) / Resolution: 3.92 Å 43532 8vul EMDB-43532, PDB-8vul: Human GluN1-2A with Fab 003-102 Local refinement of ATD Method: EM (single particle) / Resolution: 3.83 Å 43534 8vun EMDB-43534, PDB-8vun: Human GluN1-2A With Fab 008-218 Method: EM (single particle) / Resolution: 4.01 Å 43536 8vuq EMDB-43536, PDB-8vuq: Human GluN1-2A with Fab 008-218 Local refinement of ATD Method: EM (single particle) / Resolution: 3.85 Å 43537 8vur EMDB-43537, PDB-8vur: Human GluN1-2A with IgG 003-102 WT conformation Method: EM (single particle) / Resolution: 3.84 Å 43538 8vus EMDB-43538, PDB-8vus: Human GluN1-2A with IgG 007-168 Method: EM (single particle) / Resolution: 3.99 Å 43539 8vut EMDB-43539, PDB-8vut: Human GluN1-2A with IgG 008-218 Method: EM (single particle) / Resolution: 3.7 Å 43540 8vuu EMDB-43540, PDB-8vuu: Human GluN1-2B with Fab 007-168 Method: EM (single particle) / Resolution: 4.05 Å 43541 8vuv EMDB-43541, PDB-8vuv: Human GluN1-2B with Fab 007-168 Local refinement of ATD Method: EM (single particle) / Resolution: 3.69 Å 43544 8vuy EMDB-43544, PDB-8vuy: Rat GluN1-2B with Fab 003-102 Method: EM (single particle) / Resolution: 3.81 Å 43559 8vvh EMDB-43559, PDB-8vvh: rat GluN1a-2B Fab 003-102 local refinement Method: EM (single particle) / Resolution: 3.95 Å
Source	homo sapiens (human) rattus norvegicus (Norway rat)
Keywords	MEMBRANE/IMMUNE SYSTEM / Receptor / antibody / ion channel / MEMBRANE-IMMUNE SYSTEM complex / MEMBRANE PROTEIN/IMMUNE SYSTEM / Channel / heterotetramer / MEMBRANE PROTEIN-IMMUNE SYSTEM complex / MEMBRANE PROTEIN