The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Crystal Structure of the Bcl-XL-Beclin 1 Peptide Complex
Open accessAbstract
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.
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Metadata
- Authors
- Oberstein, A., Jeffrey, P. D., & Shi, Y.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-04
- Volume
- 282
- Issue
- 17
- Pages
- 13123-13132
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2108198510
- Cited by
- 563
- References
- 10
- FWCI
- 16.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
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