BAG protein
From Proteopedia
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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=''> | ||
| - | The '''BAG family proteins''' ('''Bcl-2 associated athanogenes''') perform diverse functions. | + | 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. |
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| + | == Structural highlights == | ||
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| + | BAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. | ||
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</StructureSection> | </StructureSection> | ||
Revision as of 08:09, 9 November 2015
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3D structures of BAG family proteins
Updated on 09-November-2015
