BAG protein: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
Line 8: | Line 8: | ||
BAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. | BAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved. | ||
==3D structures of BAG family proteins== | |||
[[BAG family proteins 3D structures]] | |||
</StructureSection> | </StructureSection> |
Revision as of 13:22, 1 April 2019
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. 3D structures of BAG family proteinsBAG family proteins 3D structures
|
|
3D structures of BAG family proteins3D structures of BAG family proteins
Updated on 01-April-2019
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