BAG protein

<StructureSection load='3fzf' size='350' side='right' caption='Structure of human BAG-1 BAG domain (green) complex with HSC70 ATPase domain (grey) and ATP (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 11-February-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