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4pd0

From Proteopedia

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Current revision

1.7 A resolution structure of gephyrin's E-domain

Structural highlights

4pd0 is a 1 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 1.7Å
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.^[1] ^[2]

Publication Abstract from PubMed

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.

Modulation of Gephyrin-Receptor Affinity by Multivalency.,Maric HM, Kasaragod VB, Schindelin H ACS Chem Biol. 2014 Aug 19. PMID:25137389^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kirsch J, Wolters I, Triller A, Betz H. Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons. Nature. 1993 Dec 23-30;366(6457):745-8. PMID:8264797 doi:http://dx.doi.org/10.1038/366745a0
↑ Stallmeyer B, Schwarz G, Schulze J, Nerlich A, Reiss J, Kirsch J, Mendel RR. The neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cells. Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1333-8. PMID:9990024
↑ Maric HM, Kasaragod VB, Schindelin H. Modulation of Gephyrin-Receptor Affinity by Multivalency. ACS Chem Biol. 2014 Aug 19. PMID:25137389 doi:http://dx.doi.org/10.1021/cb500303a

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4pd0"

Categories: Large Structures | Rattus norvegicus | Kasaragod VB | Maric HM | Schindelin H

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4pd0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PD0 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pd0 OCA], [https://pdbe.org/4pd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pd0 RCSB], [https://www.ebi.ac.uk/pdbsum/4pd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pd0 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pd0 OCA], [https://pdbe.org/4pd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pd0 RCSB], [https://www.ebi.ac.uk/pdbsum/4pd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pd0 ProSAT]</span></td></tr>
 </table>
 == Function ==

4pd0

From Proteopedia

Current revision

1.7 A resolution structure of gephyrin's E-domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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