BAG protein: Difference between revisions

Revision as of 10:11, 28 March 2018

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 28-March-2018

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

[1]

@@ Line 55: / Line 55: @@
 **[[4eew]] – hBAG-6 UBL domain <br />
-**[[4wwr]], [[4x86]] – hBAG-6 + ubiquitin-like protein 4A <br />
+**[[2n9p]] – hBAG-6 UBL domain + RNF126<br />
+**[[6au8]] – hBAG-6 residues 1008-1050 + TRC35 <br />
+**[[4wwr]], [[4x86]] – hBAG-6 residues 1054-1105 + ubiquitin-like protein 4A <br />
 }}
 == References ==
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 [[Category: Topic Page]]