1cy5: Difference between revisions

Revision as of 21:45, 30 June 2008

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File:1cy5.png

Template:STRUCTURE 1cy5

CRYSTAL STRUCTURE OF THE APAF-1 CARDCRYSTAL STRUCTURE OF THE APAF-1 CARD

Template:ABSTRACT PUBMED 10543941

About this StructureAbout this Structure

1CY5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-'''CRYSTAL STRUCTURE OF THE APAF-1 CARD'''
+===CRYSTAL STRUCTURE OF THE APAF-1 CARD===
-==Overview==
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-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.
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 ==About this Structure==
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 [[Category: Greek key topology]]
 [[Category: Six alpha-helix bundle]]
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