BAG protein

Function

The BAG family proteins (Bcl-2 associated athanogenes) or BAG-family molecular chaperone protein perform diverse functions. 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. ^[1]

Structural highlights

BAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved.

3D structures of BAG family proteins

BAG family proteins 3D structures

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

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Kabbage M, Dickman MB. The BAG proteins: a ubiquitous family of chaperone regulators. Cell Mol Life Sci. 2008 May;65(9):1390-402. doi: 10.1007/s00018-008-7535-2. PMID:18264803 doi:http://dx.doi.org/10.1007/s00018-008-7535-2

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Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Kabbage M, Dickman MB. The BAG proteins: a ubiquitous family of chaperone regulators. Cell Mol Life Sci. 2008 May;65(9):1390-402. doi: 10.1007/s00018-008-7535-2. PMID:18264803 doi:http://dx.doi.org/10.1007/s00018-008-7535-2

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