4tk4

GephE in complex with a GABA receptor alpha3 subunit derived double mutant peptide in space group P61

spinqualitylabelsall models 4tk4, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tk4 is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.601Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GEPH_RAT Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Publication Abstract from PubMed gamma-Aminobutyric acid type A and glycine receptors (GABAARs, GlyRs) are the major inhibitory neurotransmitter receptors and contribute to many synaptic functions, dysfunctions and human diseases. GABAARs are important drug targets regulated by direct interactions with the scaffolding protein gephyrin. Here we deduce the molecular basis of this interaction by chemical, biophysical and structural studies of the gephyrin-GABAAR alpha3 complex, revealing that the N-terminal region of the alpha3 peptide occupies the same binding site as the GlyR beta subunit, whereas the C-terminal moiety, which is conserved among all synaptic GABAAR alpha subunits, engages in unique interactions. Thermodynamic dissections of the gephyrin-receptor interactions identify two residues as primary determinants for gephyrin's subunit preference. This first structural evidence for the gephyrin-mediated synaptic accumulation of GABAARs offers a framework for future investigations into the regulation of inhibitory synaptic strength and for the development of mechanistically and therapeutically relevant compounds targeting the gephyrin-GABAAR interaction. Molecular basis of the alternative recruitment of GABAA versus glycine receptors through gephyrin.,Maric HM, Kasaragod VB, Hausrat TJ, Kneussel M, Tretter V, Stromgaard K, Schindelin H Nat Commun. 2014 Dec 22;5:5767. doi: 10.1038/ncomms6767. PMID:25531214 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gephyrin

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