BAG protein

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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 (PDB entry [[3fzf]])' scene=''>
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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=''>
The '''BAG family proteins''' ('''Bcl-2 associated athanogenes''') perform diverse functions. They contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. '''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.
The '''BAG family proteins''' ('''Bcl-2 associated athanogenes''') perform diverse functions. They contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. '''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.

Revision as of 11:01, 14 August 2014

Structure of human BAG-1 BAG domain (green) complex with HSC70 ATPase domain (grey) and ATP (stick model) (PDB entry 3fzf)

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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