3SAJ

Crystal Structure of glutamate receptor GluA1 Amino Terminal Domain

Summary for 3SAJ

• Entry DOI: 10.2210/pdb3saj/pdb
• Descriptor: Glutamate receptor 1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: rossmann fold, ion channel, membrane, transport protein
• Biological source: Rattus norvegicus (rat)
• Total number of polymer chains: 4
• Total formula weight: 183906.44

Authors

Jin, R.,Zong, Y.,Yao, G.,Gu, S. (deposition date: 2011-06-02, release date: 2011-06-22, Last modification date: 2024-11-20)

Primary citation

Yao, G.,Zong, Y.,Gu, S.,Zhou, J.,Xu, H.,Mathews, I.I.,Jin, R.
Crystal structure of the glutamate receptor GluA1 N-terminal domain.
Biochem.J., 438:255-263, 2011

PubMed Abstract: The AMPA (α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid) subfamily of iGluRs (ionotropic glutamate receptors) is essential for fast excitatory neurotransmission in the central nervous system. The malfunction of AMPARs (AMPA receptors) has been implicated in many neurological diseases, including Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis. The active channels of AMPARs and other iGluR subfamilies are tetramers formed exclusively by assembly of subunits within the same subfamily. It has been proposed that the assembly process is controlled mainly by the extracellular ATD (N-terminal domain) of iGluR. In addition, ATD has also been implicated in synaptogenesis, iGluR trafficking and trans-synaptic signalling, through unknown mechanisms. We report in the present study a 2.5 Å (1 Å=0.1 nm) resolution crystal structure of the ATD of GluA1. Comparative analyses of the structure of GluA1-ATD and other subunits sheds light on our understanding of how ATD drives subfamily-specific assembly of AMPARs. In addition, analysis of the crystal lattice of GluA1-ATD suggests a novel mechanism by which the ATD might participate in inter-tetramer AMPAR clustering, as well as in trans-synaptic protein-protein interactions.

PubMed: 21639859
DOI: 10.1042/BJ20110801

Experimental method

X-RAY DIFFRACTION (2.5 Å)