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1pq1
From Proteopedia
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Crystal structure of Bcl-xl/Bim
Overview
After antigen-driven expansion, the majority of T cells involved in an, immune response die rapidly by apoptosis dependent on the Bcl-2 related, proteins, Bim and Bax or Bak. The details of how these proteins are, activated and interact are still unclear. The crystal structure of mouse, Bcl-x(L) bound to a long helical fragment of Bim indicates that the, structure of Bim is very different from proteins with a Bcl-2-like fold, and may leave the BH3 region of Bim constitutively exposed. Based on the, structural homology between Bcl-x(L) and Bax, we predicted that binding of, Bim to Bax would require displacement of the Bax penultimate alpha helix., Consistent with this prediction, truncation of this short helix was, required for Bim/Bax interaction and led to spontaneous activation of Bax., Our results suggest a way in which both Bim and Bax/Bak might be required, for activated T cell apoptosis.
About this Structure
1PQ1 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
The structure of a Bcl-xL/Bim fragment complex: implications for Bim function., Liu X, Dai S, Zhu Y, Marrack P, Kappler JW, Immunity. 2003 Sep;19(3):341-52. PMID:14499110
Page seeded by OCA on Wed Nov 21 00:01:00 2007
Categories: Mus musculus | Protein complex | Dai, S. | Kappler, J.W. | Liu, X. | Marrack, P. | Zhu, Y. | Bcl-xl/bim
