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4GPA

High resolution structure of the GluA4 N-terminal domain (NTD)

Summary for 4GPA
Entry DOI10.2210/pdb4gpa/pdb
Related3hsy 3o21
DescriptorGlutamate receptor 4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordspbp fold, glutamate receptor, ligand-gated ion channel, ion transport, transmembrane ampa receptor regulating proteins, tarps, cornichons, ckamp44, glycosylation, rna editing, cell membrane, synapse, extracellular space, transport protein
Biological sourceRattus norvegicus (brown rat,rat,rats)
Total number of polymer chains1
Total formula weight45617.44
Authors
Sukumaran, M.,Greger, I.H. (deposition date: 2012-08-20, release date: 2012-10-24, Last modification date: 2020-07-29)
Primary citationDutta, A.,Shrivastava, I.H.,Sukumaran, M.,Greger, I.H.,Bahar, I.
Comparative Dynamics of NMDA- and AMPA-Glutamate Receptor N-Terminal Domains.
Structure, 20:1838-1849, 2012
Cited by
PubMed Abstract: Ionotropic glutamate receptors (iGluRs) harbor two extracellular domains: the membrane-proximal ligand-binding domain (LBD) and the distal N-terminal domain (NTD). These are involved in signal sensing: the LBD binds L-glutamate, which activates the receptor channel. Ligand binding to the NTD modulates channel function in the NMDA receptor subfamily of iGluRs, which has not been observed for the AMPAR subfamily to date. Structural data suggest that AMPAR NTDs are packed into tight dimers and have lost their signaling potential. Here, we assess NTD dynamics from both subfamilies, using a variety of computational tools. We describe the conformational motions that underly NMDAR NTD allosteric signaling. Unexpectedly, AMPAR NTDs are capable of undergoing similar dynamics; although dimerization imposes restrictions, the two subfamilies sample similar, interconvertible conformational subspaces. Finally, we solve the crystal structure of AMPAR GluA4 NTD, and combined with molecular dynamics simulations, we characterize regions pivotal for an as-yet-unexplored dynamic spectrum of AMPAR NTDs.
PubMed: 22959625
DOI: 10.1016/j.str.2012.08.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

226707

數據於2024-10-30公開中

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