3ygs

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[[Image:3ygs.gif|left|200px]]
[[Image:3ygs.gif|left|200px]]
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{{Structure
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|RELATEDENTRY=[[2ygs|2YGS]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ygs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ygs OCA], [http://www.ebi.ac.uk/pdbsum/3ygs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3ygs RCSB]</span>
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'''APAF-1 CARD IN COMPLEX WITH PRODOMAIN OF PROCASPASE-9'''
'''APAF-1 CARD IN COMPLEX WITH PRODOMAIN OF PROCASPASE-9'''
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[[Category: Srinivasula, S.]]
[[Category: Srinivasula, S.]]
[[Category: Wu, G.]]
[[Category: Wu, G.]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: caspase activation]]
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[[Category: Caspase activation]]
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[[Category: caspase recruitment]]
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[[Category: Caspase recruitment]]
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[[Category: recognition complex]]
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[[Category: Recognition complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:15:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:36:42 2008''
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Revision as of 19:15, 4 May 2008

Template:STRUCTURE 3ygs

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


Overview

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.

About this Structure

3YGS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1., Qin H, Srinivasula SM, Wu G, Fernandes-Alnemri T, Alnemri ES, Shi Y, Nature. 1999 Jun 10;399(6736):549-57. PMID:10376594 Page seeded by OCA on Sun May 4 22:15:41 2008

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