BAG protein: Difference between revisions

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**[[4eew]] – hBAG-6 UBL domain <br />
**[[4eew]] – hBAG-6 UBL domain <br />
**[[4wwr]], [[4x86]] – hBAG-6 + ubiquitin-like protein 4A <br />
}}
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[[Category: Topic Page]]
[[Category: Topic Page]]

Revision as of 14:28, 3 March 2015


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.

Structure of human BAG-1 BAG domain (green) complex with HSC70 ATPase domain (grey) and ATP (stick model) (PDB entry 3fzf)

Drag the structure with the mouse to rotate

3D structures of BAG family proteins3D structures of BAG family proteins

Updated on 03-March-2015

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman