3i4w | pdb_00003i4w

Crystal Structure of the third PDZ domain of PSD-95

spinqualitylabelsall models 3i4w, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3i4w is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT NonStd Res: SNN Resources: FirstGlance, OCA, RCSB, PDBsum Function [DLG4_HUMAN] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of the third PDZ domain of the neuronal post-synaptic density-95 protein (PSD95-PDZ3, residues 302-402) has been solved at 1.4 and 1.35A from two different crystal forms. These structures lack the cloning artefact present in the carboxyl terminal sequence of the former crystallographic structures and they belong to the space groups P4(3) and P1. The new PDZ structures are identical between the two crystal forms and among the four chains of the P1 crystal form. When we compare the new structures with the previous ones, some important conformational differences in the C-terminal alpha-helix and in the loop connecting beta2 and beta3 strands have been found. Additionally, the high resolution of the new structures has allowed us to indentify a succinimide residue at the position corresponding to Asp332 in the beta2-beta3 loop, which may contribute to the alternate conformation of this loop, and at the same time, to the interaction between residues from this loop and the C-terminal alpha-helix. Thus, these features would have implications in the recently proposed allosteric role of this third alpha-helix in the binding of the carboxyl terminal fragments to the PSD95-PDZ3. Novel conformational aspects of the third PDZ domain of the neuronal post-synaptic density-95 protein revealed from two 1.4A X-ray structures.,Camara-Artigas A, Murciano-Calles J, Gavira JA, Cobos ES, Martinez JC J Struct Biol. 2010 Jun;170(3):565-9. Epub 2010 Mar 19. PMID:20227506 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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