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1ohu
From Proteopedia
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| - | [[Image:1ohu.jpg|left|200px]] | + | [[Image:1ohu.jpg|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF CAENORHABDITIS ELEGANS CED-9''' | + | {{Structure |
| + | |PDB= 1ohu |SIZE=350|CAPTION= <scene name='initialview01'>1ohu</scene>, resolution 2.03Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF CAENORHABDITIS ELEGANS CED-9''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OHU is a [ | + | 1OHU is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12894216 12894216] |
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ced-9]] | [[Category: ced-9]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:10 2008'' |
Revision as of 11:11, 20 March 2008
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| , resolution 2.03Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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