BAG protein: Difference between revisions

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== Function ==
== Function ==
      
      
The '''BAG family proteins''' ('''Bcl-2 associated athanogenes''') 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. <ref>PMID:18264803</ref>
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. <ref>PMID:18264803</ref>


== Structural highlights ==
== Structural highlights ==

Latest revision as of 11:45, 2 May 2020


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

  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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Michal Harel, Alexander Berchansky, Joel L. Sussman