BAG protein: Difference between revisions

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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=''>
<StructureSection load='' 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 ==
      
      
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''') or '''BAG-family molecular chaperone protein''' 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. <ref>PMID:18264803</ref>


==3D structures of BAG family proteins==
== Structural highlights ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
BAG proteins contain a common BAG domain ca. 45 amino acid long near the C terminal which is conserved.


'''BAG-1'''
==3D structures of BAG family proteins==
 
[[BAG family proteins 3D structures]]
[[1i6z]] – mBAG-1 BAG domain - mouse<br />
[[2lwp]] – mBAG-1 BAG domain - NMR<br />
[[1t7s]] – BAG-1 BAG domain – Caenorhabditis elegans<br />
[[4hwc]] – AtBAG-1 BAG domain – Arabidopsis thaliana<br />
[[1wxv]] – hBAG-1 BAG domain – human - NMR<br />
 
'''BAG-1 complex with HSC70'''
 
[[3fzf]] – hBAG-1 BAG domain + HSC70 ATPase domain + ATP<br />
[[3fzh]], [[3fzk]],  [[3fzl]], [[3fzm]], [[3ldq]], [[3m3z]] – hBAG-1 BAG domain + HSC70 ATPase domain + inhibitor<br />
[[4hwi]] – AtBAG-1 BAG domain + HSC70 ATPase domain <br />
[[1hx1]] – BAG-1 BAG domain + HSC70 ATPase domain - bovine<br />
 
'''BAG-2'''
 
[[3d0t]] – mBAG-2 BAG domain <br />
 
 
'''BAG-2 complex with HSC70'''
 
[[3cqx]] – mBAG-2 BAG domain + HSC70 ATPase domain <br />
 
'''BAG-4'''
 
[[1m62]], [[1m7k]] – hBAG-4 BAG domain - NMR<br />
 
'''BAG-5'''
 
[[1ugo]] – mBAG-5 BAG domain - NMR<br />
[[2d9d]] – hBAG-5 BAG domain - NMR<br />
 
'''BAG-5 complex with HSC70'''
 
[[3a8y]] – hBAG-5 BAG domain + HSC70 ATPase domain <br />
 
'''BAG-6'''


[[4eew]] – hBAG-6 UBL domain <br />
</StructureSection>


== References ==
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Latest revision as of 11:45, 2 May 2020


Function

The BAG family proteins (Bcl-2 associated athanogenes) or BAG-family molecular chaperone protein 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.

3D structures of BAG family proteins

BAG family proteins 3D structures


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

ReferencesReferences

  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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Michal Harel, Alexander Berchansky, Joel L. Sussman