BAG protein: Difference between revisions
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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'> | ||
== 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. | |||
==3D structures of BAG family proteins== | |||
[[BAG family proteins 3D structures]] | |||
[[ | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category: Topic Page]] | [[Category: Topic Page]] |
Latest revision as of 11:45, 2 May 2020
FunctionThe 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 highlightsBAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. 3D structures of BAG family proteinsBAG family proteins 3D structures
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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