<StructureSection load='3fzf' size='350' side='right' caption='Structure of human BAG-1 BAG domain (green) complex with HSC70 ATPase domain (grey) and ATP (stick model) (PDB entry 3fzf)' scene=>
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 proteins3D structures of BAG family proteins
Updated on 18-November-2014
{"openlevels":0}
- 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
- BAG-2 complex with HSC70
- 3cqx – mBAG-2 BAG domain + HSC70 ATPase domain
- BAG-4
- 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
proteopedia link