2p1l
From Proteopedia
|
Structure of the Bcl-XL:Beclin 1 complex
Overview
Bcl-2 family proteins are key regulators of apoptosis and have recently, been shown to modulate autophagy. The tumor suppressor Beclin 1 has been, proposed to coordinate both apoptosis and autophagy through direct, interaction with anti-apoptotic family members Bcl-2 and/or Bcl-X(L)., However, the molecular basis for this interaction remains enigmatic. Here, we report that Beclin 1 contains a conserved BH3 domain, which is both, necessary and sufficient for its interaction with Bcl-X(L). We also report, the crystal structure of a Beclin BH3 peptide in complex with Bcl-X(L) at, 2.5A resolution. Reminiscent of previously determined Bcl-X(L)-BH3, structures, the amphipathic BH3 helix of Beclin 1 bound to a conserved, hydrophobic groove of Bcl-X(L). These results define Beclin 1 as a novel, BH3-only protein, implying that Beclin 1 may have a direct role in, initiating apoptotic signaling. We propose that this putative apoptotic, function may be linked to the ability of Beclin 1 to suppress tumor, formation in mammals.
About this Structure
2P1L is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein., Oberstein A, Jeffrey PD, Shi Y, J Biol Chem. 2007 Apr 27;282(17):13123-32. Epub 2007 Mar 2. PMID:17337444
Page seeded by OCA on Wed Jan 23 14:59:19 2008
