GLUD2 Antibody
- Known as:
- GLUD2 Antibody
- Catalog number:
- GWB-MT567I
- Product Quantity:
- 50ug
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- GLUD2 Antibody
Related genes to: GLUD2 Antibody
- Gene:
- GLUD2 NIH gene
- Name:
- glutamate dehydrogenase 2
- Previous symbol:
- GLUDP1
- Synonyms:
- -
- Chromosome:
- Xq24
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-10-05
Related products to: GLUD2 Antibody
Related articles to: GLUD2 Antibody
- The glutamate delta receptors GluD1 and GluD2 are part of the ionotropic glutamate receptor (iGluR) family; however, delta receptors differ from other iGluRs as they do not bind glutamate. These receptors have important and diverse functions in the brain and are known to be involved in various neurological diseases. Here, we report the monomeric X-ray crystal structure of the ligand-binding domain of rat GluD1 (rGluD1-LBD) with D-serine and Zn ions, determined at 2.8 Å resolution. By comparing the structures with Zn ions (rGluD1-LBD) and Ca ions (human, hGluD1-LBD), we show that species and crystallization differences do not affect intermediate domain closure and D-serine interactions with GluD1. Furthermore, examining the effect of replacing the Ca ions in the hGluD1-LBD dimer with Mg, Zn or Na ions did not reveal significant differences in the overall structure of the hGluD1-LBD for the different cations. We show that the cations were coordinated by the same residues, Glu527, Val530 and Asp531, and several water molecules. In the structure of hGluD1-LBD, Cl ions are present at the dimer interface and molecular dynamics (MD) simulations showed that removal of the ions leads to opening of the dimer, highlighting the importance of Cl ions in stabilizing the dimer. Finally, MD simulations of hGluD1-LBD and the Pro725 to Ser725 mutant, with and without D-serine in the binding site, suggest that Pro725 hinders full domain closure in GluD1, whereas an apparent synergistic effect of D-serine and mutation to Ser725 leads to a significant interlobe closure of the clamshell-like structure. - Source: PubMed
Publication date: 2026/08/16
Jørgensen Flemming SteenPedersen Emma GrosvaldNarayanan DilipFrydenvang Karla AKastrup Jette Sandholm - Chemical modification of proteins is an important tool for the development of protein-based therapeutics, a rapidly growing field in disease treatment. Currently, no universal approach exists for site-specifically introducing desired functionalities into proteins with minimal disruption. Here, we present a reactive peptide tag/probe pair system for site-specific covalent protein labeling, leveraging the interaction between a lysine-containing histidine tag (KH6 or H6K) and a binuclear nickel (II)-nitrilotriacetic acid (BisNi²+-NTA) probe conjugated to a lysine-reactive N-acyl-N-alkyl sulfonamide (NASA) electrophilic group. This chapter describes the system's validation, preparation of a glutamate receptor δ2 (GluD2) targeting nanobody-biotin conjugate, and its functional assessment via live-cell imaging of GluD2. The method offers a versatile, efficient approach for protein labeling applicable to protein engineering and targeted therapeutics. - Source: PubMed
Thimaradka VikramTamura TomonoriHamachi Itaru - Alzheimer's disease (AD) involves not only amyloid-β and tau pathology but synaptic dysfunction and impaired autophagy, though the underlying mechanisms and their relationship to AD progression are not well understood. Transsynaptic complexes involving presynaptic neurexins (Nrxn1/2/3), secreted cerebellins (Cbln1/2/3/4), and postsynaptic glutamate delta receptors (GluD1/2) play critical roles in organizing synapses and synaptic plasticity. Studies in pain models have reported that treatment with recombinant Cbln1 rescues AMPA glutamate receptor imbalance, promotes autophagy, and inhibits hyperexcitability and pain behaviors. Here we tested the novel hypothesis that dysregulation of Cbln-GluD-based transsynaptic complexes may occur in the brain of AD patients, providing insights into disease progression and potential avenues for therapeutic development. - Source: PubMed
Publication date: 2026/06/10
Hindle AshlyChen YongYin XianglingManczak MariaDecourt BorisNeugebauer Volker - The GluD1 receptor has many unusual features including expression at both excitatory and inhibitory synapses and a ligand binding domain capable of binding both D-serine and GABA. We have previously demonstrated that striatal GluD1 is critical for the regulation of behavioral flexibility, a phenotype dependent on the cholinergic system. Here, we found that GluD1 is enriched postsynaptically at cholinergic synapses in the mouse and monkey dorsal striatum. Further, loss of GluD1 reduces the abundance of cholinergic terminals, excitatory responses at cholinergic synapses as well as muscarinic receptor-induced plasticity. In addition, optogenetic stimulation of cholinergic interneurons or puff-application of ACh, in the presence of cholinergic and AMPA/GABA receptor blockers, produced current responses in medium spiny neurons (MSNs) that were sensitive to the GluD1-channel blocker NASPM. These responses were absent in GluD1 KO and overexpression of GluD1 on KO background rescued Ach puff-induced currents suggesting potential conductance via GluD1. Finally, using GluD1-Cbln1 interaction assay as an indirect method to evaluate ligand binding interaction, we found that ACh can bind GluD1 and induce conformational changes. A similar ACh-induced conformational change was observed for GluD2 in the cell binding assay. Importantly, molecular dynamics simulations and mutagenesis analysis demonstrated that ACh binding orientation in the GluD1 ligand binding domain is different from D-serine and GABA. Overall, our results identified an unprecedented feature of GluD1 in the regulation of cholinergic synapses. - Source: PubMed
Publication date: 2026/06/10
Chettiar Poojashree BS Narasimhan Kishore KumarSabnis Siddhesh SEricksen Spencer SChoi DianeSmith YolandDravid Shashank M - The delta-type ionotropic glutamate receptors (iGluRs) GluD1 and GluD2 are ligand-gated ion channels that are fundamental for regulating both excitatory and inhibitory synapses. Rising evidence points to the role of GluD1 in the development of neurological diseases. However, the ultrastructure of human GluD1 (hGluD1) and the molecular basis for its ligand-gating remain unclear. Here, we define the structure of hGluD1 and resolve its ligand-gating mechanism using cryo-electron microscopy (cryoEM) and single channel bilayer recording. While hGluD1 exhibits a non-swapped architecture, it contains conserved iGluR moieties that enable ligand-gating, such as a ligand-binding domain (LBD) tethered to a transmembrane ion channel. Binding of the neurotransmitter γ-aminobutyric acid (GABA) or D-serine to the LBD enables cation influx through the hGluD1 ion channel. Our findings delineate the molecular architecture and function of hGluD1, provide foundations for understanding patient mutations in hGluD1, and will invigorate therapeutic development against hGluD1. - Source: PubMed
Publication date: 2026/04/08
Mondal Anish KumarWang HaoboWeaver Mae GZheng IrisKormshchikov NikitaAhmed FairineTwomey Edward C