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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 2.03Å" /> '''STRUCTURE OF CAENORH...)
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Revision as of 20:50, 20 November 2007
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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
Page seeded by OCA on Tue Nov 20 22:57:47 2007
