This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3ygs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2ygs|2YGS]]
 +
|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>
}}
}}
Line 33: Line 36:
[[Category: recognition complex]]
[[Category: recognition complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:07:47 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:36:42 2008''

Revision as of 02:36, 31 March 2008


PDB ID 3ygs

Drag the structure with the mouse to rotate
, resolution 2.5Å
Related: 2YGS


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 Mon Mar 31 05:36:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools