4pd0

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pd0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pd0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pd0 PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pd0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pd0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pd0 PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
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Gephyrin is a major determinant for the accumulation and anchoring of glycine receptors (GlyRs) and the majority of gamma-aminobutyric acid type A receptors (GABAARs) at postsynaptic sites. Here we explored the interaction of gephyrin with a dimeric form of a GlyR beta-subunit receptor-derived peptide. A 2 A crystal structure of the C-terminal domain of gephyrin (GephE) in complex with a 15-residue peptide derived from the GlyR beta-subunit defined the core binding site which we targeted with the dimeric peptide. Biophysical analyses via differential scanning calorimetry (DSC), thermofluor and isothermal titration calorimetry (ITC) demonstrated that this dimeric ligand is capable of binding simultaneously to two receptor binding sites and that this multivalency results in a 25-fold enhanced affinity. Our study therefore suggests that the oligomeric state of gephyrin and the number of gephyrin-binding subunits in the pentameric GABAARs and GlyRs together control postsynaptic receptor clustering.
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Modulation of Gephyrin-Receptor Affinity by Multivalency.,Maric HM, Kasaragod VB, Schindelin H ACS Chem Biol. 2014 Aug 19. PMID:25137389<ref>PMID:25137389</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
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Revision as of 03:13, 4 September 2014

1.7 A resolution structure of gephyrin's E-domain

4pd0, resolution 1.70Å

Drag the structure with the mouse to rotate

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