1CWW

SOLUTION STRUCTURE OF THE CASPASE RECRUITMENT DOMAIN (CARD) FROM APAF-1

Summary for 1CWW

• Entry DOI: 10.2210/pdb1cww/pdb
• Descriptor: APOPTOTIC PROTEASE ACTIVATING FACTOR 1 (1 entity in total)
• Functional Keywords: helical bundle, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O14727
• Total number of polymer chains: 1
• Total formula weight: 11511.16

Authors

Day, C.L.,Dupont, C.,Lackmann, M.,Vaux, D.L.,Hinds, M.G. (deposition date: 1999-08-26, release date: 2000-01-21, Last modification date: 2024-05-22)

Primary citation

Day, C.L.,Dupont, C.,Lackmann, M.,Vaux, D.L.,Hinds, M.G.
Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1.
Cell Death Differ., 6:1125-1132, 1999

PubMed Abstract: Activation of procaspase-9, a key component of the apoptosis mechanism, requires the interaction of its caspase recruitment domain (CARD) with the CARD in the adaptor protein Apaf-1. Using nuclear magnetic resonance spectroscopy and mutagenesis we have determined the structure of the CARD from Apaf-1 and the residues important for binding the CARD in procaspase-9. Apaf-1's CARD contains seven short alpha-helices with the core six helices arranged in an antiparallel manner. Residues in helix 2 have a central role in mediating interaction with procaspase-9 CARD. This interaction surface is distinct from that proposed based on the structure of the CARD from RAIDD, but is coincident with that of the structurally similar FADD death effector domain and the Apaf-1 CARD interface identified by crystallographic studies.

PubMed: 10578182
DOI: 10.1038/sj.cdd.4400584

Experimental method

SOLUTION NMR