|
|
| Line 1: |
Line 1: |
| [[Image:2p1l.gif|left|200px]] | | {{Seed}} |
| | [[Image:2p1l.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2p1l| PDB=2p1l | SCENE= }} | | {{STRUCTURE_2p1l| PDB=2p1l | SCENE= }} |
|
| |
|
| '''Structure of the Bcl-XL:Beclin 1 complex'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17337444}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17337444 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_17337444}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| [[Category: Beclin]] | | [[Category: Beclin]] |
| [[Category: Bh3 domain]] | | [[Category: Bh3 domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:08:53 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:19:58 2008'' |
