Ionotropic Glutamate Receptors

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Revision as of 09:18, 14 July 2019

spinqualitylabelsall models Structure of the ionotropic glutamate receptor tetramer, GluA2, (3kg2) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image       Contents 1 Introduction 1.1 Involvement in Autism Spectrum Disorders 1.2 GluA2 Structure 1.2.1 The Amino Terminal Domain 1.2.2 The Transmembrane Domain 1.2.3 The Ligand Binding Domain 1.3 Pharmaceutical Relevance 2 3D structures of glutamate receptor Introduction Ionotropic Glutamate Receptors (IGluRs) are a family of ligand-gated ion channels that are responsible for fast excitatory neurotransmission.[1] Primarily localized to nerve synapses in mammals, IGluRs are implicated in nearly all aspects of nervous system development and function.[2] Synapses form the connection between two neuronal cells. Within synapses, neurotransmitters are released from vesicles in presynaptic cells and interact with receptors in postsynaptic cells to allow for communication between nerve cells.[1] GluR domains include the amino terminal domain (ATD), transmembrane domain (TMD) and ligand-binding domain (LBD). Glutamate is the predominant neurotransmitter of excitatory synapses and interacts specifically with AMPA and NMDA IGluRs.[3] AMPA receptor is a non-NMDA-type IGluR Kainate receptor (GluK) is a non-NMDA-type IGluR which is activated by the agonist kainate. NMDA receptor (NMDAR) is a IGluR which binds to the agonist NMDA. It contains subuntis NR1, NR2A, NR2B, NR2C, NR2D, NR3A, NR3B. Additional details in Molecular Playground/Glutamate Receptor Metabotropic glutamate receptor Glutamate receptor (GluA2) Neurodevelopmental Disorders Ligand Binding N-Terminal of Metabotropic Glutamate Receptors. Involvement in Autism Spectrum Disorders       Autism Spectrum Disorders (ASDs) are neurodevelopmental disorders. During development, glutamate regulates neuronal growth and synaptogenesis, effectively dictating the underlying connective neuronal architecture of the brain.[3] Significant research into ASDs has been devoted to understanding how glutamate receptors function and how disruption leads to neurodevelopmetnal disorders. IGluRs are concentrated in regions of the brain that have been implicated in ASDs including the cerebellum and hippocampus. These are the areas responsible for motor control, spatial navigation and memory, attributes that are often disrupted in patients with ASDs. Studies have revealed that glutamate receptor expression is increased in the cerebellum of autistic individuals by nearly 250%. A number of small nucleotide polymorphisms in IGluRs have also been identified which correlate with the ASDs. Further, many people with autism have clearly visible disturbances in the inferior olive (IO) in the brain. The IO plays a critical role in movement coordination and maintenance of an underlying 12 Hz brain rhythm through careful regulation of glutamate signaling.[4] A well-known mouse model called “Lurcher” for the lurching type movements the mice make has served as an important model for studying ASDs. The mutation that causes the “Lurcher” phenotype creates a constitutively leaky glutamate receptor ion channel resulting in IO neuron degeneration and loss of purkinje cells. These mice exhibit some of the well-known Autism-like characteristics.[5] Such relationships between overly active glutamate receptors leading to increased excitation/inhibition ratios and autism have led some to propose using glutamate receptor inhibitors as a means of pharmaceutical intervention for improving those with autistic symptoms.[6] Many pharmacological agents that reduce neural excitation, such as benzodiazapines, are thought to potentially have therapeutic value in treating autistic symptoms.[3] GluA2 Structure       AMPA IGluRs form composed of and . Each subunit includes an extracellular (ATD) which is responsible for receptor trafficking within the membrane, a (LBD) which activates the receptor upon binding glutamate, and a (TMD) which forms the membrane-spanning ion channel. Also present is a carboxy-terminal domain involved in receptor localization and regulation, although the structure of this domain has not been solved.[2] The structure of AMPA IGluRs or in this case GluA2, is unique in that the . The ATD has a local two-fold symmetry, the LBD has a two-fold symmetry, while the TMD has a four-fold symmetry. Here is a morph depicting the . This symmetry mismatch has implications for function of the receptor with subunits behaving differently depending upon their orientation despite identical primary sequence.[2] For an excellent analysis, see: Glutamate Receptor Symmetry Analysis The Amino Terminal Domain       is responsible for receptor assembly, trafficking and localization. It has two unique sets of interactions which hold the tetramer together. The is present in each pair of dimers and involves both hydrogen bonding and hydrophobic interactions. The , which includes residues Ile 203, Thr 204, Ile 205, and Val 209 on both chains among others, effectively holds the pair of dimers together at an angle that is roughly 24 degrees off of the overall two-fold axis.[2][7] The Transmembrane Domain       has a pore structure that is nearly identical to that of the Potassium Channel. With complete four-fold symmetry, 16 helices form a through which cations can flow through. In the current, inhibitor bound structure, the at a highly conserved , with Thr 617, Ala 621, and Thr 625 occluding the ion permeation pathway.[2] The of the channel includes the residues Thr 625, Ala 621, and Thr 617, but does not distinguish between positive cations like in the Potassium Channel. Located next to this narrow region lies , which is replaced with a threonine in the Lurcher mouse model mentioned previously. This mutation, which introduces a much bulkier residue, prevents the helices from closing properly, resulting in a constitutively open ion channel.[2] The Ligand Binding Domain       is located just above the TMD and has an overall . Within each LBD lies the so-called . This structure is responsible for and “sensitizing” the receptor to allow passage of cations through the channel. Residues Pro 89, Leu 90, Arg 96, Ser 142, & Glu 193 among others (residue numbers in 1ftj model), which are responsible for within the clamshell, are highly conserved. Glutamate binding causes a () in the LBD which pulls the M3 helices in the TMD apart, opening the channel and allowing for cation passage. A morph of the conformational change in the LBD upon glutamate binding can be . Uniquely, due to the varied importance of the homotetramer subunits due to symmetry mismatch, the interaction of glutamate with the distal subunits is predicted to result in a greater conformational change. Thus these distal subunits play a more critical role in channel sensitization and activation.[2] Pharmaceutical Relevance       As mentioned previously, extensive investigation into the pharmaceutical potential of IGluRs as a target for treating various ailments including Autism Spectrum Disorders symptoms is ongoing. In addition to agents which reduce neural excitation such as benzodiazapines, small molecules that potentiate AMPA receptor currents have been proven to reduce cognitive deficits caused by neurodegenerative diseases such as Alzheimer's Disease.[3] Modulators such as aniracetam and CX614 (2al4) of the ligand-binding core through interactions with a “proline ceiling” and a “serine floor”, stabilizing the closed-clamshell conformation. Although these compounds would likely be ineffective in the case of Autism patients because they slow the deactivation of the IGluR channels, this class of compounds has exciting therapeutic potential.[1]. The glutamate receptor inhibitor Diuril is used as drug in cases of hypertension, edema, diabetes insipidus and kidney stones[8]. 3D structures of glutamate receptor Glutamate receptor 3D structures

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This article was developed based on lectures given in Chemistry 543 by Prof. Clarence E. Schutt at Princeton University.

3D structures of glutamate receptor

Updated on 14-July-2019 {{#tree:id=OrganizedByTopic|openlevels=0|

• GluR domains: ATD 1-393; LBD 394-544; TMD 545-908

• Ionotropic glutamate receptor 0

• • 2pyy - IGluR2 LBD + Glu – Nostoc punctiforme

• Ionotropic glutamate receptor 1

• • 3saj - rIGluR1 ATD – rat
    
  • 5ict – DmIGluR1 LBD (mutant) – Drosophila melanogaster
    
  • 5dt6 – DmIGluR1 LBD (mutant) + glutamate
    
  • 4io2 – AvIGluR1 LBD + Glu – Adineta vaga
    
  • 4io3, 4io4, 4io5, 4io6, 4io7 – AvIGluR1 LBD + amino acid
    

• Ionotropic glutamate receptor 2

• • 2wjw, 2wjx – hIGluR2 ATD - human
    
  • 3rn8, 3rnn – hIGluR2 LBD + potentiator
    
  • 5ybg, 5ybf - hIGluR2 LBD + potentiator + Glu
    
  • 4u1y, 4u2p, 5l1b - rIGluR2
    
  • 5vov, [[5vou, 5vot - rIGluR2 + calcium channel γ-2 – Cryo EM
    
  • 3n6v, 3o2j, 5n6p - rIGluR2 ATD (mutant) – rat
    
  • 3hsy, 3h5v, 3h5w - rIGluR2 ATD
    
  • 3bki, 5l1e, 5l1f 5l1e, 5l1f, 5l1g, 5l1h - rIGluR2 LBD + inhibitor
    
  • 1fto, 4h8j - rIGluR2 LBD
    
  • 3t93, 4u2r - rIGluR2 LBD (mutant)
    
  • 5fth, 5fti, 5ns9 - rIGluR2 LBD (mutant) + Glu
    
  • 5kk2, 5vov, 5vou, 5vot - rIGluR2 + calcium channel γ2 subunit – Cryo-EM
    

• GluR2 positive allosteric modulator complex

• • 2xhd, 5h8s - hIGluR2 LBD + positive allosteric modulator + Glu
    
  • 3pmv, 3pmw, 3pmx, 3o28, 3o29, 3o2a, 3o6g, 3o6h, 3o6i, 3m3l, 3lsl, 3tdj - rIGluR2 LBD + positive allosteric modulator + Glu
    
  • 2al4, 1p1o - rIGluR2 LBD (mutant) + positive allosteric modulator
    
  • 3ijo, 3ijx, 3il1, 3ilt, 3ilu, 3lsl, 3tdj, 5oew, 6hch, 6hcc, 6hcb, 6hc9, 6faz - rIGluR2 + positive allosteric modulator + Glu
    
  • 2xx8, 2xx7, 2xx9, 2xxh, 2xxi, 3lsf, 3h6t, 3h6u, 3h6v, 3h6w, 3bbr, 3tkd, 4fat, 4iy5, 4iy6, 4lz5, 4lz7, 4lz8, 4n07, 5o9a - rIGluR2 LBD (mutant) + positive allosteric modulator + Glu
    
  • 1mm6, 1mm7, 6hca - rIGluR2 LBD + positive allosteric modulator
    
  • 3ik6 - rIGluR2 + Duiril + Glu
    

• GluR2 antagonist complex

• • 3r7x, 6fqk, 6fqj, 6fqi - hIGluR2 LBD + antagonist
    
  • 6fqh, 6fqg - hIGluR2 LBD (mutant) + antagonist
    
  • 3kgc, 3kg2, 2cmo - rIGluR2 LBD + antagonist + Glu
    
  • 4u4g - rIGluR2 + antagonist
    

A topic page describing in detail the GluA2 structure described in 3kg2

• • 3h03, 3h06, 3b7d, 1n0t, 1ftl, 3tza, 3ua8, 4isu, 5cbs, 5cbr, 4yma - rIGluR2 LBD + antagonist
    
  • 1lb9, 4l17, 4u21, 4u22, 4u23, 5kbv - rIGluR2 LBD (mutant) + antagonist
    

• GluR2 agonist complex

• • 3rtf, 3rtw, 3pd8, 3pd9, 3bft, 3bfu, 1wvj, 1syh, 1syi, 1ms7, 1mqd, 1nnp, 1nnk, 1m5b, 1m5c, 1m5d, 1m5e, 1m5f, 1ftm, 4g8m, 4igt, 5vhw, 5vhx, 5vhy, 5vhz, 5fho, 5fhn, 5fhm, 4x48, 4q30, 5nih, 5ng9, 6q60, 6q54 - rIGluR2 LBD + agonist
    
  • 3b6t, 2al5, 2anj, 1p1q, 1p1u, 1p1w, 1lb8 - rIGluR2 LBD (mutant) + agonist
    
  • 1lbc, 5elv - rIGluR2 LBD (mutant) + agonist + Glu
    
  • 2p2a, 5buu, 6hch, 6hcc, 6hcb - rIGluR2 LBD + agonist + Glu
    

• GluR2 partial agonist complex

• • 5zg2 - hIGluR2 + partial agonist
    
  • 5zg3, 5zg1, 5zg0, 5ybg, 5ybf - hIGluR2 + partial agonist + Glu
    
  • 4u4f - rIGluR2 + partial agonist
    
  • 1y1m, 2aix, 1y1z, 1y20, 1mqg, 1mqh, 1mqi, 1mqj, 1mxu, 1mxv, 1mxw, 1mxx, 1mxy, 1mxz, 1my0, 1my1, 1my2, 1my3, 1my4, 1fw0, 1ftk, 1gr2 - rIGluR2 LBD + partial agonist
    
  • 1xhy, 1p1n, 1lbb, 3t96, 3t9h, 3t9u, 3t9v, 5jei - rIGluR2 LBD (mutant) + partial agonist
    
  • 4u2q - rIGluR2 + partial agonist
    
  • 4u5b, 4u5c, 4u5d, 4u5e, 4u5f - rIGluR2 + partial agonist + snail toxin + modulator
    
  • 4gxs, 4u1o, 4u1w, 4u1x, 4u1z - rIGluR2 LBD + kainate derivative
    

• GluR2 ligand complex

• • 3dp6, 2uxa, 2i3v, 2i3w, 1ftj, 4z0i, 4o3b, 6gl4 - rIGluR2 LBD + Glu
    
  • 3b6q, 3b6w, 2gfe, 3t9x, 4u4s, 4u4x, 4yu0, 6giv - rIGluR2 LBD (mutant) + Glu
    
  • 4o3a, 4o3c - rIGluR2 LBD + Asp
    
  • 4u1o, 4u1w, 4u1x, 4u1z - rIGluR2 LBD + kainate derivative
    
  • 4uqk, 4uqj, 4uq6 - rIGluR2 + quisqualate – Cryo EM
    
  • 4wxj - DmIGluR2 LBD + Glu
    

• Ionotropic glutamate receptor δ

• • 5kc8 – hIGluRδ2 ATD
    
  • 5kc9 – IGluRδ1 C-terminal - mouse
    
  • 5l2e – rIGluRδ2
    
  • 5cc2 – rIGluRδ2 LBD + agonist
    

• Ionotropic glutamate receptor 1+2

• • 6qkz, 6qkc – rIGluR1 + rGluR2 + calcium channel g-8 – Cryo EM
    
  • 6njl – rIGluR1 + rGluR2 + calcium channel g-8 + auxiliary protein + antibody – Cryo EM
    

• Ionotropic glutamate receptor 1+2+3

• • 6njn – rIGluR1 + rGluR2 + rIGluR3 + calcium channel g-8 + auxiliary protein + antibody – Cryo EM
    

• Ionotropic glutamate receptor 2+3

• • 5ide, 5idf, 5fwy – rIGluR2 + rGluR3
    
  • 6njm – rGluR2 + rIGluR3 + calcium channel γ-8 + auxiliary protein + antibody – Cryo EM
    

• Ionotropic glutamate receptor 2+4

• • 5fwx – rIGluR2 ATD + rIGluR4 ATD
    

• Ionotropic glutamate receptor 3

• • 3o21, 3p3w, 6fpj, 6flr – rIGluR3 ATD
    
  • 3m3k – rIGluR3 LBD
    
  • 3rt6, 3rt8, 3dp4 – rIGluR3 LBD + agonist
    
  • 3m3f – rIGluR3 LBD + allosteric modulator
    
  • 3dln - rIGluR3 LBD + Glu
    
  • 4f1y - rIGluR3 LBD + CNQX
    
  • 4f22, 4f39, 4f3g - rIGluR3 LBD + kainate
    
  • 4f31 - rIGluR3 LBD (mutant) + kainate
    
  • 4f29 - rIGluR3 LBD + quisqualate
    
  • 4f2o, 4f2q - rIGluR3 LBD (mutant) + quisqualate
    
  • 4f3b - rIGluR3 LBD (mutant) + Glu
    

• Ionotropic glutamate receptor 4

• • 3epe, 3fas - rIGluR4 LBD + Glu
    
  • 3kei – rIGluR4 LBD (mutant) + Glu
    
  • 3kfm - rIGluR4 LBD (mutant) + partial agonist
    
  • 3en3 - rIGluR4 LBD + partial agonist
    
  • 3fat – rIGluR4 LBD + agonist
    
  • 4gpa – rIGluR4 ATD
    

• Ionotropic glutamate receptor 5

• • 3fuz, 2zns – hIGluR5 LBD + Glu
    
  • 3fv1, 3fv2, 3fvg, 3fvk, 3fvn, 3fvo, 2znt, 2znu - hIGluR5 LBD + agonist
    
  • 1txf - rIGluR5 LBD + Glu
    
  • 2ojt - rIGluR5 + anion
    
  • 3c31, 3c32, 3c33, 3c34, 3c35, 3c36 - rIGluR5 LBD + ion
    
  • 2wky, 3gba, 3gbb, 2pbw, 2f34, 2f35, 2f36 – rIGluR5 LBD + agonist
    
  • 2qs1, 2qs2, 2qs3, 2qs4 - rIGluR5 LBD (mutant) + agonist
    
  • 1vso - rIGluR5 LBD + antagonist
    

• Ionotropic glutamate receptor 6

• • 3h6g, 3h6h – rIGluR6 ATD
    
  • 3g3f, 1sd3, 1s50, 1s7y – rIGluR6 LBD + Glu
    
  • 3g3g, 3g3h, 3g3i, 3g3j, 3g3k, 2i0b, 2i0c - rIGluR6 LBD (mutant) + Glu
    
  • 1s9t – rIGluR6 LBD + positive allosteric modulator
    
  • 1tt1 – rIGluR6 LBD + partial agonist
    

• Metabotropic glutamate receptor see Metabotropic glutamate receptor

• Ionotropic kainate receptor 1

• • 1ycj – rGluK1 LBD + Glu
    
  • 5nf5, 5neb – rGluK1 LBD + Glu analog
    
  • 3s2v, 4dld, 5m2v, 4ymb, 4qf9, 4mf3, 6fz4 – rGluK1 LBD + antagonist
    
  • 4e0x – rGluK1 LBD + kainate
    
  • 5mfq, 5mfv, 5mfw – rGluK1 LBD + kainite + allosteric modulator
    

• Ionotropic kainate receptor 2

• • 3qxm - hGluK2 LBD + toxin
    
  • 2xxr – rGluK2 LBD + Glu
    
  • 4h8i, 5cmm - rGluK2 LBD + Glu derivative
    
  • 2xxu, 2xxx, 2xxw, 4bdl, 4bdn, 4bdq, 5cmk – rGluK2 LBD (mutant) + Glu
    
  • 4bdm, 4bdo, 4bdr – rGluK2 LBD (mutant) + kainate
    
  • 2xxt – rGluK2 LBD + partial agonist
    
  • 2xxv, 2xxy – rGluK2 LBD (mutant) + partial agonist
    
  • 3qlt - rGluK2 residues 32-420 (mutant)
    
  • 1yae, 5kuf - rGluK2 LBD + agonist
    
  • 5kuh - rGluK2 LBD (mutant) + agonist
    
  • 4uqq - rGluK2 ATD,LBD,TMD (mutant) + agonist
    

• Ionotropic kainate receptor 3

• • 3olz – rGluK3 ATD
    
  • 3s9e, 3u93, 3u94, 4mh5 – rGluK3 LBD + Glu
    
  • 5nf6 - rGluK3 LBD + Glu analog
    
  • 3u92, 4e0w - rGluK3 LBD + kainate
    
  • 4g8n, 4igr, 4nwd, 4nwc, 5o4f - rGluK3 LBD + agonist
    
  • 6f29, 6f28 - rGluK3 LBD + pyrimidine derivative
    

• Ionotropic kainate receptor 4

• • 5ikb – rGluK4 LBD + kainate
    

• Ionotropic kainate receptor 5

• • 3om0, 3om1 – rGluK5 ATD
    
  • 3qlu - rGluK5 + rGluK2 (mutant)
    
  • 3qlv - rGluK5 + rGluK2

• NMDA receptor (NMDAR)

• NMDAR subunit NR1

• • 2nr1 – hNMDAR TMD - NMR
    
  • 4kcc – rNMDAR LBD
    
  • 3q41 – rNMDAR N ATD
    
  • 1y1m, 1y1z, 1y20 – NMDAR LBD (mutant) + partial agonist
    
  • 2hqw – NMDAR C terminal + calmodulin
    
  • 1pb7 – rNMDAR LBD + glycine
    
  • 1pb8, 1pb9 – rNMDAR LBD + serine
    
  • 1pbq – rNMDAR LBD + DCKA
    
  • 4kfq – rNMDAR LBD + antagonist
    
  • 5fxk, 5fxi, 5fxh, 5fxg – rNMDAR (mutant) – Cryo EM
    
  • 3qek – XlNMDA R ATD (mutant) – Xenopus laevis
    

• NMDAR subunit NR2A

• • 2a5s - rNMDAR LBD + glutamate
    
  • 4jwx – rNMDAR LBD + agonist
    

• NMDAR subunit NR2B

• • 3jpy, 3jpw - rNMDAR ATD (mutant)
    
  • 5up2, 5uow - XlNMDAR + NR2A + Fab + glutamate – Cryo-EM
    
  • 5un1 - XlNMDAR + methyl-aspartate receptor + glutamate
    

• NMDAR subunit NR3A

• • 4kcd – rNMDAR LBD
    
  • 2rc8 - rNMDAR LBD + serine
    
  • 2rc7, 2rca - rNMDAR LBD + glycine
    
  • 2rc9 - rNMDAR LBD + ACPC
    

• NMDAR subunit NR3B

• • 2rcb - rNMDAR LBD + serine
    

• NMDAR subunit NR2D

• • 4jwy – rNMDAR LBD + agonist
    
  • 3oek, 3oem – rNMDAR LBD + aspartate
    
  • 3oel, 3oen – rNMDAR LBD + glutamate
    

• NMDAR subunit NR1+NR2A

• • 5h8f – hNMDAR LBD
    
  • 6mmx, 6mmw, 6mmv, 6mmu, 6mmt, 6mms, 6mmr, 6mmp, 6mmn, 6mmm, 6mml, 6mmk, 6mmj, 6mmi, 6mmh, 6mmg, 6mmb, 6mma, 6mm9, 6irh, 6irg, 6irf, 6ira – rNMDAR ATD+LBD+TMD – Cryo EM
    
  • 4nf4, 4nf5, 4nf6, 4nf8, 2a5t – rNMDAR LBD
    
  • 5tpz – XlNMDAR ATD
    

• NMDAR subunit NR1+NR2A complex

• • 5tpa, 5tp9 – hNMDAR LBD + antagonist
    
  • 5kdt, 5kcj – hNMDAR LBD + modulator
    
  • 5tpa, 5tp9, 5kdt, 5kcj, 5i2n, 5i2k, 5h8q, 5h8n, 5h8h – hNMDAR LBD + allosteric modulator
    
  • 5vij, 5vii, 5vih, 5dex, 5u8c – rNMDAR LBD + antagonist
    
  • 5vij, 5vii, 5vih, 5u8c – rNMDAR LBD+TMD + antagonist
    
  • 5jty, 5fxj – rNMDAR + agonist
    
  • 5tq0, 5tq2 – rNMDAR LBD + antibody
    
  • 5i59, 5i58, 5i57, 5i56 – rNMDAR LBD + allosteric modulator
    
  • 5tq2, 5tq0, 5tpw – XlNMDAR1 ATD (mutant) + rNMDAR2A LBD + antibody
    
  • 5tpw – XlNMDAR1 LBD (mutant) + rNMDAR2A LBD + antibody
    
  • 5ewm, 5ewl – XlNMDAR1 ATD (mutant) + rNMDAR2A ATD (mutant) + antagonist
    

• NMDAR subunit NR1+NR2B

• • 6cna – rNMDAR ATD+LBD+TMD – Cryo EM
    
  • 5tpz – rNMDAR LBD
    
  • 4pe5, 4tll, 4tlm – rNMDAR (mutants)
    
  • 5b3j – XlNMDAR1 ATD (mutant) + rNMDAR2B ATD (mutant) + antibody
    
  • 5un1 – XlNMDAR LBD+TMD
    
  • 5ipv, 5ipt, 5ips, 5ipr, 5ipq, 5iov, 5iou – rNMDAR2B (mutant) + NMDAR1 + inhibitor
    
  • 5ipu, 6e7x, 6e7w, 6e7v, 6e7u, 6e7t, 6e7s, 6e7r – XlNMDAR2B (mutant) + NMDAR1 (mutant) + inhibitor
    
  • 3qel, 3qem, 5ewj – XlNMDAR ATD (mutant) + ifenprodil
    

• NMDAR subunit NR1+NR2A+NR2B

• • 5up2, 5uow – XlNMDAR + antibody – Cryo EM
    

}}

Topic Page on Glutamate Receptor GluA2 structure

There is a topic page describing in detail the GluA2 structure described in 3kg2. The page is meant to complement the original publication of the structure by Sobolevsky et al.^[2][9] with matching colors, etc..

See Also

• Glutamate Receptor Symmetry Analysis
  
• Glutamate receptor (GluA2) structure in detail
  
• Metabotropic glutamate receptor
  
• Membrane Channels & Pumps
  
• Alzheimer's Disease
  

References

1. ↑ ^{1.0 1.1 1.2} Jin R, Clark S, Weeks AM, Dudman JT, Gouaux E, Partin KM. Mechanism of positive allosteric modulators acting on AMPA receptors. J Neurosci. 2005 Sep 28;25(39):9027-36. PMID:16192394 doi:25/39/9027
2. ↑ ^{2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7} Sobolevsky AI, Rosconi MP, Gouaux E. X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature. 2009 Dec 10;462(7274):745-56. Epub . PMID:19946266 doi:10.1038/nature08624
3. ↑ ^{3.0 3.1 3.2 3.3} Purcell AE, Jeon OH, Zimmerman AW, Blue ME, Pevsner J. Postmortem brain abnormalities of the glutamate neurotransmitter system in autism. Neurology. 2001 Nov 13;57(9):1618-28. PMID:11706102
4. ↑ Welsh JP, Ahn ES, Placantonakis DG. Is autism due to brain desynchronization? Int J Dev Neurosci. 2005 Apr-May;23(2-3):253-63. PMID:15749250 doi:10.1016/j.ijdevneu.2004.09.002
5. ↑ Zuo J, De Jager PL, Takahashi KA, Jiang W, Linden DJ, Heintz N. Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene. Nature. 1997 Aug 21;388(6644):769-73. PMID:9285588 doi:10.1038/42009
6. ↑ Rubenstein JL, Merzenich MM. Model of autism: increased ratio of excitation/inhibition in key neural systems. Genes Brain Behav. 2003 Oct;2(5):255-67. PMID:14606691
7. ↑ Jin R, Singh SK, Gu S, Furukawa H, Sobolevsky AI, Zhou J, Jin Y, Gouaux E. Crystal structure and association behaviour of the GluR2 amino-terminal domain. EMBO J. 2009 Jun 17;28(12):1812-23. Epub 2009 May 21. PMID:19461580 doi:10.1038/emboj.2009.140
8. ↑ HERRMANN GR, HEJTMANCIK MR, GRAHAM RN, MARBURGER RC. A new superior oral diuretic drug, chlorothiazide (diuril); clinical evaluation. Tex State J Med. 1958 Sep;54(9):639-45. PMID:13580922
9. ↑ Wollmuth LP, Traynelis SF. Neuroscience: Excitatory view of a receptor. Nature. 2009 Dec 10;462(7274):729-31. PMID:20010675 doi:10.1038/462729a