BAG protein: Difference between revisions
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<StructureSection load='3fzf' size='350' side='right' caption='Structure of human BAG-1 BAG domain (green) complex with HSC70 ATPase domain (grey) and ATP (stick model) (PDB entry [[3fzf]])' scene=''> | <StructureSection load='3fzf' size='350' side='right' caption='Structure of human BAG-1 BAG domain (green) complex with HSC70 ATPase domain (grey) and ATP (stick model) (PDB entry [[3fzf]])' scene='56/568986/Cv/1'> | ||
== Function == | == Function == |
Revision as of 15:31, 13 January 2016
FunctionThe 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. [1] Structural highlightsBAG 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 proteins3D structures of BAG family proteins
Updated on 13-January-2016
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