BAG protein: Difference between revisions

Revision as of 23:46, 18 October 2017

Function

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. ^[1]

Structural highlights

BAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved.

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

Drag the structure with the mouse to rotate

3D structures of BAG family proteins3D structures of BAG family proteins

Updated on 18-October-2017

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] 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

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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='56/568986/Cv/1'>		<StructureSection load='3fzf' 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 ==		== Function ==