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| <scene name='80/800120/Cv/5'>Para-Phenyl crosslinked Glycine receptor beta subunit derived dimeric peptide</scene> interacts with several side chains of Gep<ref>PMID:25413248</ref>. | | <scene name='80/800120/Cv/5'>Para-Phenyl crosslinked Glycine receptor beta subunit derived dimeric peptide</scene> interacts with <scene name='80/800120/Cv/8'>several side chains of Gep</scene><ref>PMID:25413248</ref>. |
| *<scene name='80/800120/Cv/7'>1,1'-benzene-1,4-diylbis(1H-pyrrole-2,5-dione) crosslinking with peptides</scene> | | *<scene name='80/800120/Cv/7'>1,1'-benzene-1,4-diylbis(1H-pyrrole-2,5-dione) crosslinking with peptides</scene> |
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Revision as of 11:34, 30 October 2018
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Function
Gephyrin (Gep) is responsible for Mo cofactor biosynthesis and for postsynaptic clustering of glycine receptors and type A GABA receptors in the vertebrate CNS. Gep self-assembles to form scaffolds in the synapse[1].
Relevance
Abnormal accumulation of Gep are highly correlated with the neuropathologic diagnosis of Alzheimer Disease[2].
Structural highlights
Para-Phenyl crosslinked Glycine receptor beta subunit derived dimeric peptide interacts with several side chains of Gep[3].
- ↑ Tyagarajan SK, Fritschy JM. Gephyrin: a master regulator of neuronal function? Nat Rev Neurosci. 2014 Mar;15(3):141-56. doi: 10.1038/nrn3670. PMID:24552784 doi:https://dx.doi.org/10.1038/nrn3670
- ↑ Hales CM, Rees H, Seyfried NT, Dammer EB, Duong DM, Gearing M, Montine TJ, Troncoso JC, Thambisetty M, Levey AI, Lah JJ, Wingo TS. Abnormal gephyrin immunoreactivity associated with Alzheimer disease pathologic changes. J Neuropathol Exp Neurol. 2013 Nov;72(11):1009-15. doi:, 10.1097/01.jnen.0000435847.59828.db. PMID:24128675 doi:https://dx.doi.org/10.1097/01.jnen.0000435847.59828.db
- ↑ Maric HM, Kasaragod VB, Haugaard-Kedstrom L, Hausrat TJ, Kneussel M, Schindelin H, Stromgaard K. Design and Synthesis of High-Affinity Dimeric Inhibitors Targeting the Interactions between Gephyrin and Inhibitory Neurotransmitter Receptors. Angew Chem Int Ed Engl. 2014 Nov 20. doi: 10.1002/anie.201409043. PMID:25413248 doi:https://dx.doi.org/10.1002/anie.201409043
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3D structures of gephyrin
Updated on 30-October-2018
2fu3, 5erq, 4pd0 - rGeph E domain 318-736 - rat
2fts, 4pd1, 1t3e, 4u91 - rGeph E domain + glycine receptor peptide
4tk1, 4tk2, 4tk3, 4tk4, 4u90 - rGeph E domain + GABA receptor peptide
5ers - rGeph E domain + AMP
5ert, 5err - rGeph E domain + ADP
5eru - rGeph E domain + ADP + Mo + MoO4
5erv - rGeph E domain + ADP + W + WO4
1thc - rGeph N terminal
References
