3ygs: Difference between revisions

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[[Image:3ygs.gif|left|200px]]
{{Seed}}
[[Image:3ygs.png|left|200px]]


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{{STRUCTURE_3ygs|  PDB=3ygs  |  SCENE=  }}  
{{STRUCTURE_3ygs|  PDB=3ygs  |  SCENE=  }}  


'''APAF-1 CARD IN COMPLEX WITH PRODOMAIN OF PROCASPASE-9'''
===APAF-1 CARD IN COMPLEX WITH PRODOMAIN OF PROCASPASE-9===




==Overview==
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Caspase-9-mediated apoptosis (programmed cell death) plays a central role in the development and homeostasis of all multicellular organisms. Mature caspase-9 is derived from its procaspase precursor as a result of recruitment by the activating factor Apaf-1. The crystal structures of the caspase-recruitment domain of Apaf-1 by itself and in complex with the prodomain of procaspase-9 have been determined at 1.6 and 2.5 A resolution, respectively. These structures and other evidence reveal that each molecule of Apaf-1 interacts with a molecule of procaspase-9 through two highly charged and complementary surfaces formed by non-conserved residues; these surfaces determine recognition specificity through networks of intermolecular hydrogen bonds and van der Waals interactions. Mutation of the important interface residues in procaspase-9 or Apaf-1 prevents or reduces activation of procaspase-9 in a cell-free system. Wild-type, but not mutant, prodomains of caspase-9 completely inhibit catalytic processing of procaspase-9. Furthermore, analysis of homologues from Caenorhabditis elegans indicates that recruitment of CED-3 by CED-4 is probably mediated by the same set of conserved structural motifs, with a corresponding change in the specificity-determining residues.
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{{ABSTRACT_PUBMED_10376594}}


==About this Structure==
==About this Structure==
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[[Category: Caspase recruitment]]
[[Category: Caspase recruitment]]
[[Category: Recognition complex]]
[[Category: Recognition complex]]
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