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.
2ygs
From Proteopedia
(New page: 200px<br /> <applet load="2ygs" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ygs, resolution 1.6Å" /> '''CARD DOMAIN FROM APA...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2ygs.gif|left|200px]]<br /> | + | [[Image:2ygs.gif|left|200px]]<br /><applet load="2ygs" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ygs" size=" | + | |
caption="2ygs, resolution 1.6Å" /> | caption="2ygs, resolution 1.6Å" /> | ||
'''CARD DOMAIN FROM APAF-1'''<br /> | '''CARD DOMAIN FROM APAF-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Caspase-9-mediated apoptosis (programmed cell death) plays a central role | + | 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== | ==About this Structure== | ||
| - | 2YGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2YGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGS OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 19: | ||
[[Category: recognition]] | [[Category: recognition]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:57:05 2008'' |
Revision as of 16:57, 21 February 2008
|
CARD DOMAIN FROM APAF-1
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
2YGS is a Single protein structure of sequence 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 Thu Feb 21 18:57:05 2008
