The BAG family proteins (Bcl-2 associated athanogenes) perform diverse functions. They contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. BAG-1, BAG-2, BAG-4, BAG-5 or BAG family molecular chaperone regulator inhibit the chaperone function of HSC70 and have anti-apoptotic function.
3D structures of BAG family proteins
Updated on 14-August-2014
BAG-1
1i6z – mBAG-1 BAG domain - mouse
2lwp – mBAG-1 BAG domain - NMR
1t7s – BAG-1 BAG domain – Caenorhabditis elegans
4hwc – AtBAG-1 BAG domain – Arabidopsis thaliana
1wxv – hBAG-1 BAG domain – human - NMR
BAG-1 complex with HSC70
3fzf – hBAG-1 BAG domain + HSC70 ATPase domain + ATP
3fzh, 3fzk, 3fzl, 3fzm, 3ldq, 3m3z – hBAG-1 BAG domain + HSC70 ATPase domain + inhibitor
4hwi – AtBAG-1 BAG domain + HSC70 ATPase domain
1hx1 – BAG-1 BAG domain + HSC70 ATPase domain - bovine
BAG-2
3d0t – mBAG-2 BAG domain
BAG-2 complex with HSC70
3cqx – mBAG-2 BAG domain + HSC70 ATPase domain
BAG-4
1m62, 1m7k – hBAG-4 BAG domain - NMR
BAG-5
1ugo – mBAG-5 BAG domain - NMR
2d9d – hBAG-5 BAG domain - NMR
BAG-5 complex with HSC70
3a8y – hBAG-5 BAG domain + HSC70 ATPase domain
BAG-6
4eew – hBAG-6 UBL domain
