Tdp-43

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TDP-43 helical stabilizers

Compound A is the best current binder to the healthy helical tdp-43 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3037571/)

Drag the structure with the mouse to rotate

3D Structures of Tdp-43

Updated on 17-March-2018

2cqg – hTDP-43 RRM1 domain – human - NMR
1wf0 – hTDP-43 RRM2 domain - NMR
5mrg, 2n4p, 5x4f – hTDP-43 N-terminal domain - NMR
5mdi – hTDP-43 N-terminal domain
2n2c, 2n3x – hTDP-43 prion-like helix - NMR
2n4g, 2n4h – hTDP-43 prion-like helix (mutant) - NMR
4y0f, 4iuf – hTDP-43 RRM1 domain + DNA
4y00 – hTDP-43 RRM1 domain (mutant) + DNA
4bs2 – hTDP-43 RRM1+RRM2 domains + RNA - NMR
3d2w – TDP-43 RRM2 domain + DNA - mouse

References

  1. Buratti E, Baralle FE. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci. 2008 Jan 1;13:867-78. PMID:17981595
  2. Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, Rogelj B, Ackerley S, Durnall JC, Williams KL, Buratti E, Baralle F, de Belleroche J, Mitchell JD, Leigh PN, Al-Chalabi A, Miller CC, Nicholson G, Shaw CE. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science. 2008 Mar 21;319(5870):1668-72. doi: 10.1126/science.1154584. Epub 2008, Feb 28. PMID:18309045 doi:10.1126/science.1154584
  3. Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, Hashizume Y, Beach TG, Buratti E, Baralle F, Morita M, Nakano I, Oda T, Tsuchiya K, Akiyama H. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol. 2008 Jul;64(1):60-70. doi: 10.1002/ana.21425. PMID:18546284 doi:http://dx.doi.org/10.1002/ana.21425

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