1pq1
From Proteopedia
(New page: 200px<br /><applet load="1pq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pq1, resolution 1.65Å" /> '''Crystal structure of...) |
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| - | [[Image:1pq1.jpg|left|200px]]<br /><applet load="1pq1" size=" | + | [[Image:1pq1.jpg|left|200px]]<br /><applet load="1pq1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pq1, resolution 1.65Å" /> | caption="1pq1, resolution 1.65Å" /> | ||
'''Crystal structure of Bcl-xl/Bim'''<br /> | '''Crystal structure of Bcl-xl/Bim'''<br /> | ||
==Overview== | ==Overview== | ||
| - | After antigen-driven expansion, the majority of T cells involved in an | + | 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== | ==About this Structure== | ||
| - | 1PQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1PQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQ1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Dai, S.]] | [[Category: Dai, S.]] | ||
| - | [[Category: Kappler, J | + | [[Category: Kappler, J W.]] |
[[Category: Liu, X.]] | [[Category: Liu, X.]] | ||
[[Category: Marrack, P.]] | [[Category: Marrack, P.]] | ||
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[[Category: bcl-xl/bim]] | [[Category: bcl-xl/bim]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:19 2008'' |
Revision as of 12:31, 21 February 2008
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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 Thu Feb 21 14:31:19 2008
Categories: Mus musculus | Protein complex | Dai, S. | Kappler, J W. | Liu, X. | Marrack, P. | Zhu, Y. | Bcl-xl/bim
