Apoptotic protease-activating factor: Difference between revisions

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<StructureSection load='5juy' size='340' side='right' caption='Human apoptosis protease-activating factor-1 (green) complex with cytochrome c (red) and caspase 9 (magenta) forming the apoptosome (PDB entry [[5juy]]) ' scene='77/774059/Cv/2'>
<StructureSection load='5juy' size='340' side='right' caption='Human apoptosis protease-activating factor-1 complex with cytochrome c and caspase 9 forming the apoptosome (PDB entry [[5juy]]) ' scene='77/774059/Cv/2'>




== Function ==
== Function ==


'''Apoptosis protease-activating factor-1''' (APAF-1) binds to cytochrome c and ATP to form the apoptosome which leads to the recruitment and activation of caspase 9 by cleaving the procaspase 9.  Caspase 9 is involved in executing the apoptosis of cells<ref>PMID:15829969</ref>.
'''Apoptosis protease-activating factor-1''' or '''Apoptosis peptidase-activating factor-1''' (APAF-1) binds to cytochrome c and ATP to form the apoptosome which leads to the recruitment and activation of caspase 9 by cleaving the procaspase 9.  Caspase 9 is involved in executing the apoptosis of cells<ref>PMID:15829969</ref>.


== Disease ==
== Disease ==
Line 13: Line 13:


Apaf-1 contains several copies of the WD-40 domain which are involved in binding to cytochrome c<ref>PMID:26014357</ref>., caspase recruitment domain (CARD) and an ATPase domain.
Apaf-1 contains several copies of the WD-40 domain which are involved in binding to cytochrome c<ref>PMID:26014357</ref>., caspase recruitment domain (CARD) and an ATPase domain.
</StructureSection>
*<scene name='77/774059/Cv/3'>Apoptosome</scene> formed by Human apoptosis protease-activating factor-1 (green; subunits A, B, C, D, E, F, G) complex with cytochrome c (red; subunits H, I, J, K, L, M, N) and caspase 9 (magenta; subunits O, P, Q, R) (PDB entry [[5juy]]).


==3D structures of apoptosis protease-activating factor-1==
==3D structures of apoptotic protease-activating factor-1==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[Apoptotic protease-activating factor-1 3D structures]]


[[2ygs]], [[1cy5]], [[2p1h]] – hAPAF-1 CARD domain – human  <br />
</StructureSection>
[[1c15]], [[1cww]] – hAPAF-1 CARD domain – NMR  <br />
[[1z6t]] – hAPAF-1 + ADP  <br />
[[3ygs]] – hAPAF-1 CARD domain + procaspase 9  <br />
[[4rhw]], [[5wvc]] – hAPAF-1 CARD domain + caspase 9  <br />
[[3j2t]], [[3jbt]] – hAPAF-1 + cytochrome c<br />
[[5juy]], [[5wve]] – hAPAF-1 + caspase 9 + cytochrome c<br />


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

Latest revision as of 11:54, 9 October 2022


Function

Apoptosis protease-activating factor-1 or Apoptosis peptidase-activating factor-1 (APAF-1) binds to cytochrome c and ATP to form the apoptosome which leads to the recruitment and activation of caspase 9 by cleaving the procaspase 9. Caspase 9 is involved in executing the apoptosis of cells[1].

Disease

Inactivation of Apaf-1 is implicated in disease progression and chemoresistance of some malignancies[2].

Structural highlights

Apaf-1 contains several copies of the WD-40 domain which are involved in binding to cytochrome c[3]., caspase recruitment domain (CARD) and an ATPase domain.

  • formed by Human apoptosis protease-activating factor-1 (green; subunits A, B, C, D, E, F, G) complex with cytochrome c (red; subunits H, I, J, K, L, M, N) and caspase 9 (magenta; subunits O, P, Q, R) (PDB entry 5juy).

3D structures of apoptotic protease-activating factor-1

Apoptotic protease-activating factor-1 3D structures


Human apoptosis protease-activating factor-1 complex with cytochrome c and caspase 9 forming the apoptosome (PDB entry 5juy)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Riedl SJ, Li W, Chao Y, Schwarzenbacher R, Shi Y. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature. 2005 Apr 14;434(7035):926-33. PMID:15829969 doi:10.1038/nature03465
  2. Furukawa Y, Sutheesophon K, Wada T, Nishimura M, Saito Y, Ishii H, Furukawa Y. Methylation silencing of the Apaf-1 gene in acute leukemia. Mol Cancer Res. 2005 Jun;3(6):325-34. PMID:15972851 doi:http://dx.doi.org/10.1158/1541-7786.MCR-04-0105
  3. Shalaeva DN, Dibrova DV, Galperin MY, Mulkidjanian AY. Modeling of interaction between cytochrome c and the WD domains of Apaf-1: bifurcated salt bridges underlying apoptosome assembly. Biol Direct. 2015 May 27;10:29. doi: 10.1186/s13062-015-0059-4. PMID:26014357 doi:http://dx.doi.org/10.1186/s13062-015-0059-4

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

Michal Harel, Joel L. Sussman, Alexander Berchansky