BAG protein
From Proteopedia
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- | <StructureSection load=' | + | <StructureSection load='' size='350' side='right' caption='Structure of human BAG-1 BAG domain (green) complex with HSC70 ATPase domain (magenta) and ATP (PDB entry [[3fzf]])' scene='56/568986/Cv/1'> |
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+ | == Function == | ||
- | The '''BAG family proteins''' ('''Bcl-2 associated athanogenes''') perform diverse functions. | + | 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 == |
- | + | BAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. | |
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- | + | ==3D structures of BAG family proteins== | |
+ | [[BAG family proteins 3D structures]] | ||
- | + | </StructureSection> | |
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- | + | == References == | |
- | + | <references/> | |
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[[Category: Topic Page]] | [[Category: Topic Page]] |
Current revision
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References
- ↑ 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