1cy5: Difference between revisions

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|PDB= 1cy5 |SIZE=350|CAPTION= <scene name='initialview01'>1cy5</scene>, resolution 1.30&Aring;
|PDB= 1cy5 |SIZE=350|CAPTION= <scene name='initialview01'>1cy5</scene>, resolution 1.30&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cy5 OCA], [http://www.ebi.ac.uk/pdbsum/1cy5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cy5 RCSB]</span>
}}
}}


Line 24: Line 27:
[[Category: Joshua-Tor, L.]]
[[Category: Joshua-Tor, L.]]
[[Category: Vaughn, D E.]]
[[Category: Vaughn, D E.]]
[[Category: BME]]
[[Category: ZN]]
[[Category: apoptosis]]
[[Category: apoptosis]]
[[Category: caspase recruitment domain]]
[[Category: caspase recruitment domain]]
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[[Category: six alpha-helix bundle]]
[[Category: six alpha-helix bundle]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:30:47 2008''

Revision as of 16:30, 30 March 2008

File:1cy5.gif


Drag the structure with the mouse to rotate
1cy5, resolution 1.30Å
Ligands: BME, ZN
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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