This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


BAG protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
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.
 +
</StructureSection>
==3D structures of BAG family proteins==
==3D structures of BAG family proteins==

Revision as of 11:24, 18 November 2014

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

Drag the structure with the mouse to rotate

3D structures of BAG family proteins

Updated on 18-November-2014

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/BAG_protein"
Personal tools