1cy5
From Proteopedia
(New page: 200px<br /> <applet load="1cy5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cy5, resolution 1.30Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1cy5.gif|left|200px]]<br /> | + | [[Image:1cy5.gif|left|200px]]<br /><applet load="1cy5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1cy5" size=" | + | |
caption="1cy5, resolution 1.30Å" /> | caption="1cy5, resolution 1.30Å" /> | ||
'''CRYSTAL STRUCTURE OF THE APAF-1 CARD'''<br /> | '''CRYSTAL STRUCTURE OF THE APAF-1 CARD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The caspase recruitment domain (CARD) of Apaf-1 binds to the CARD of | + | The caspase recruitment domain (CARD) of Apaf-1 binds to the CARD of caspase-9 to trigger a proteolytic cascade that leads to apoptotic cell death. We report the crystal structure of the Apaf-1 CARD at 1. 3 A resolution, solved in a two-element multiwavelength anomalous dispersion (MAD) X-ray diffraction experiment. This CARD adopts a six-helix bundle fold with Greek key topology surrounding an extensive hydrophobic core. This fold, which we call the "death fold", is found in other domains that mediate interactions in apoptotic signaling despite very low sequence identity. From a structure-based alignment, we identify conserved patterns that characterize the death fold and its subclasses. Like the Ig-fold, it provides a rigid structural scaffold upon which diverse recognition surfaces are assembled. |
==About this Structure== | ==About this Structure== | ||
| - | 1CY5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CY5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CY5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Joshua-Tor, L.]] | [[Category: Joshua-Tor, L.]] | ||
| - | [[Category: Vaughn, D | + | [[Category: Vaughn, D E.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: six alpha-helix bundle]] | [[Category: six alpha-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:55 2008'' |
Revision as of 10:10, 21 February 2008
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CRYSTAL STRUCTURE OF THE APAF-1 CARD
Overview
The caspase recruitment domain (CARD) of Apaf-1 binds to the CARD of caspase-9 to trigger a proteolytic cascade that leads to apoptotic cell death. We report the crystal structure of the Apaf-1 CARD at 1. 3 A resolution, solved in a two-element multiwavelength anomalous dispersion (MAD) X-ray diffraction experiment. This CARD adopts a six-helix bundle fold with Greek key topology surrounding an extensive hydrophobic core. This fold, which we call the "death fold", is found in other domains that mediate interactions in apoptotic signaling despite very low sequence identity. From a structure-based alignment, we identify conserved patterns that characterize the death fold and its subclasses. Like the Ig-fold, it provides a rigid structural scaffold upon which diverse recognition surfaces are assembled.
About this Structure
1CY5 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling., Vaughn DE, Rodriguez J, Lazebnik Y, Joshua-Tor L, J Mol Biol. 1999 Oct 29;293(3):439-47. PMID:10543941
Page seeded by OCA on Thu Feb 21 12:10:55 2008
