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	Development and characterization of functional antibodies targeting NMDA receptors.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 923, Year 2022
Publish date	Feb 17, 2022
Authors	Nami Tajima / Noriko Simorowski / Remy A Yovanno / Michael C Regan / Kevin Michalski / Ricardo Gómez / Albert Y Lau / Hiro Furukawa /
PubMed Abstract	N-methyl-D-aspartate receptors (NMDARs) are critically involved in basic brain functions and neurodegeneration as well as tumor invasiveness. Targeting specific subtypes of NMDARs with distinct ...N-methyl-D-aspartate receptors (NMDARs) are critically involved in basic brain functions and neurodegeneration as well as tumor invasiveness. Targeting specific subtypes of NMDARs with distinct activities has been considered an effective therapeutic strategy for neurological disorders and diseases. However, complete elimination of off-target effects of small chemical compounds has been challenging and thus, there is a need to explore alternative strategies for targeting NMDAR subtypes. Here we report identification of a functional antibody that specifically targets the GluN1-GluN2B NMDAR subtype and allosterically down-regulates ion channel activity as assessed by electrophysiology. Through biochemical analysis, x-ray crystallography, single-particle electron cryomicroscopy, and molecular dynamics simulations, we show that this inhibitory antibody recognizes the amino terminal domain of the GluN2B subunit and increases the population of the non-active conformational state. The current study demonstrates that antibodies may serve as specific reagents to regulate NMDAR functions for basic research and therapeutic objectives.
External links	Nat Commun / PubMed:35177668 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.456 - 7.51 Å
Structure data	25843 7te9 EMDB-25843, PDB-7te9: Cryo-EM structure of GluN1b-2B NMDAR complexed to Fab2 class1 Method: EM (single particle) / Resolution: 3.92 Å 25844 7teb EMDB-25844, PDB-7teb: Cryo-EM structure of GluN1b-2B NMDAR complexed to Fab2 non-active1-like Method: EM (single particle) / Resolution: 4.23 Å 25845 7tee EMDB-25845, PDB-7tee: Cryo-EM structure of GluN1b-2B NMDAR complexed to Fab2 Non-active2-like Method: EM (single particle) / Resolution: 6.59 Å 25849 7teq EMDB-25849, PDB-7teq: Cryo-EM structure of GluN1b-2B NMDAR in complex with Fab5 active conformation Method: EM (single particle) / Resolution: 7.51 Å 25850 7ter EMDB-25850, PDB-7ter: Cryo-EM structure of GluN1b-2B NMDAR in complex with Fab5 non-active2 conformation Method: EM (single particle) / Resolution: 5.23 Å 25851 7tes EMDB-25851, PDB-7tes: Cryo-EM structure of GluN1b-2B NMDAR in complex with Fab5 in Non-active1 conformation Method: EM (single particle) / Resolution: 4.7 Å 25852 7tet EMDB-25852, PDB-7tet: Cryo-EM structure of GluN1b-2B NMDAR in complex with Fab5 in non-active2-like conformation Method: EM (single particle) / Resolution: 4.45 Å PDB-7te4: Crystal structure of Fab2 anti-GluN2B antibody Method: X-RAY DIFFRACTION / Resolution: 2.456 Å PDB-7te6: Crystal structure of GluN1b-2B ATD complexed to Fab5 anti-GluN2B antibody Method: X-RAY DIFFRACTION / Resolution: 4.55 Å
Chemicals	ChemComp-HOH: WATER
Source	rattus norvegicus (Norway rat) Mouse (mice) mus musculus (house mouse) xenopus laevis (African clawed frog)
Keywords	IMMUNE SYSTEM / Fab fragment / SIGNALING PROTEIN/IMMUNE SYSTEM / Fab fragment complexed to the receptor / SIGNALING PROTEIN-IMMUNE SYSTEM complex / Channel / antibody