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1ohu

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(New page: 200px<br /><applet load="1ohu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ohu, resolution 2.03&Aring;" /> '''STRUCTURE OF CAENORH...)
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[[Image:1ohu.jpg|left|200px]]<br /><applet load="1ohu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ohu, resolution 2.03&Aring;" />
caption="1ohu, resolution 2.03&Aring;" />
'''STRUCTURE OF CAENORHABDITIS ELEGANS CED-9'''<br />
'''STRUCTURE OF CAENORHABDITIS ELEGANS CED-9'''<br />
==Overview==
==Overview==
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The interactions between B-cell lymphoma 2 (BCL-2) family members are, known to be mediated through the binding of the BH3 domain of a, proapoptotic member to the BH3-binding groove of an antiapoptotic member., We determined the crystal structure of antiapoptotic CED-9, which reveals, a unique C-terminal helix altering the common BH3-binding region. A, coexpression system to produce CED-9 in complex with proapoptotic EGL-1, enabled us to show that the binding of EGL-1 to CED-9 is extremely stable, raising the melting temperature (T(M)) of CED-9 by 25 degrees C, and that, the binding surface of CED-9 extends beyond the BH3-binding region and, reaches the BH4 domain. Consistently, the T(M) and a 1H-15N correlation, NMR spectrum of CED-9 in complex with EGL-1 are drastically different from, those of CED-9 in complex with the EGL-1 BH3 peptide. The data suggest, that the recognition between other BCL-2 family members may also involve, much wider protein surfaces than is previously thought.
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The interactions between B-cell lymphoma 2 (BCL-2) family members are known to be mediated through the binding of the BH3 domain of a proapoptotic member to the BH3-binding groove of an antiapoptotic member. We determined the crystal structure of antiapoptotic CED-9, which reveals a unique C-terminal helix altering the common BH3-binding region. A coexpression system to produce CED-9 in complex with proapoptotic EGL-1 enabled us to show that the binding of EGL-1 to CED-9 is extremely stable, raising the melting temperature (T(M)) of CED-9 by 25 degrees C, and that the binding surface of CED-9 extends beyond the BH3-binding region and reaches the BH4 domain. Consistently, the T(M) and a 1H-15N correlation NMR spectrum of CED-9 in complex with EGL-1 are drastically different from those of CED-9 in complex with the EGL-1 BH3 peptide. The data suggest that the recognition between other BCL-2 family members may also involve much wider protein surfaces than is previously thought.
==About this Structure==
==About this Structure==
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1OHU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OHU OCA].
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1OHU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHU OCA].
==Reference==
==Reference==
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[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ha, N.C.]]
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[[Category: Ha, N C.]]
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[[Category: Jeong, J.S.]]
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[[Category: Jeong, J S.]]
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[[Category: Oh, B.H.]]
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[[Category: Oh, B H.]]
[[Category: apoptosis]]
[[Category: apoptosis]]
[[Category: bcl-2 family]]
[[Category: bcl-2 family]]
[[Category: ced-9]]
[[Category: ced-9]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:57:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:56 2008''

Revision as of 12:18, 21 February 2008


1ohu, resolution 2.03Å

Drag the structure with the mouse to rotate

STRUCTURE OF CAENORHABDITIS ELEGANS CED-9

Overview

The interactions between B-cell lymphoma 2 (BCL-2) family members are known to be mediated through the binding of the BH3 domain of a proapoptotic member to the BH3-binding groove of an antiapoptotic member. We determined the crystal structure of antiapoptotic CED-9, which reveals a unique C-terminal helix altering the common BH3-binding region. A coexpression system to produce CED-9 in complex with proapoptotic EGL-1 enabled us to show that the binding of EGL-1 to CED-9 is extremely stable, raising the melting temperature (T(M)) of CED-9 by 25 degrees C, and that the binding surface of CED-9 extends beyond the BH3-binding region and reaches the BH4 domain. Consistently, the T(M) and a 1H-15N correlation NMR spectrum of CED-9 in complex with EGL-1 are drastically different from those of CED-9 in complex with the EGL-1 BH3 peptide. The data suggest that the recognition between other BCL-2 family members may also involve much wider protein surfaces than is previously thought.

About this Structure

1OHU is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions., Woo JS, Jung JS, Ha NC, Shin J, Kim KH, Lee W, Oh BH, Cell Death Differ. 2003 Dec;10(12):1310-9. PMID:12894216

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