1pq0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1pq0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pq0, resolution 2.20&Aring;" /> '''Crystal structure of...)
Line 1: Line 1:
-
[[Image:1pq0.jpg|left|200px]]<br /><applet load="1pq0" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1pq0.jpg|left|200px]]<br /><applet load="1pq0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pq0, resolution 2.20&Aring;" />
caption="1pq0, resolution 2.20&Aring;" />
'''Crystal structure of mouse Bcl-xl'''<br />
'''Crystal structure of mouse Bcl-xl'''<br />
==Overview==
==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.
+
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==
-
1PQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PQ0 OCA].
+
1PQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1PQ0 OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dai, S.]]
[[Category: Dai, S.]]
-
[[Category: Kappler, J.W.]]
+
[[Category: Kappler, J W.]]
[[Category: Liu, X.]]
[[Category: Liu, X.]]
[[Category: Marrack, P.]]
[[Category: Marrack, P.]]
Line 20: Line 20:
[[Category: bcl-xl]]
[[Category: bcl-xl]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:00:55 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:17 2008''

Revision as of 12:31, 21 February 2008

Image:1pq0.jpg

1pq0, resolution 2.20Å

Drag the structure with the mouse to rotate

Crystal structure of mouse Bcl-xl

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

1PQ0 is a Single protein structure of sequence 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 14:31:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pq0"
Personal tools