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PMID: 16434054 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly.

Journal of molecular biology ·Vol. 357 ·No. 2 ·2006-03-24 ·Pages 358-64

Park HH, Wu H

Abstract

Caspase-2 is implicated in stress-induced apoptosis that acts as an upstream initiator of mitochondrial permeabilization. Recent studies have shown that caspase-2 activation requires a molecular complex known as the PIDDosome comprising the p53-inducible protein PIDD, the adapter protein RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain (CARD) that interacts with the CARD of caspase-2 and a C-terminal death domain (DD) that interacts with the DD in PIDD. As a first step towards elucidating the molecular mechanisms of caspase-2 activation, we report the crystal structure of RAIDD DD at 2.0 A resolution. The high-resolution structure reveals important features of RAIDD DD that may be important for DD folding and dynamics and for assembly of the PIDDosome.

MeSH Terms
Adaptor Proteins, Signal Transducing/chemistry,genetics Amino Acid Sequence Animals Apoptosis/physiology CRADD Signaling Adaptor Protein Carrier Proteins/chemistry,metabolism Caspase 2 Caspases/metabolism Crystallography, X-Ray Death Domain Receptor Signaling Adaptor Proteins Enzyme Activation Fas-Associated Death Domain Protein Humans Models, Molecular Molecular Sequence Data Multiprotein Complexes Protein Conformation Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Adaptor Proteins, Signal Transducing CRADD Signaling Adaptor Protein CRADD protein, human Carrier Proteins Death Domain Receptor Signaling Adaptor Proteins FADD protein, human Fas-Associated Death Domain Protein Multiprotein Complexes PIDD1 protein, human Caspase 2 Caspases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Park Hyun Ho
Department of Biochemistry, Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021, USA.
Wu Hao
References (36)
36 references, click to expand
  1. Molecular mechanisms of caspase regulation during apoptosis.
    Nat Rev Mol Cell Biol. 2004 Nov;5(11):897-907 PMID: 15520809
  2. Caspases and apoptosis.
    Essays Biochem. 2002;38:9-19 PMID: 12463158
  3. Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas.
    J Biol Chem. 2004 Jan 9;279(2):1474-81 PMID: 14573612
  4. Surface salt bridges stabilize the GCN4 leucine zipper.
    Protein Sci. 1998 Nov;7(11):2431-7 PMID: 9828010
  5. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.
    Cell. 1995 May 19;81(4):505-12 PMID: 7538907
  6. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons.
    Proteins. 1991;11(4):281-96 PMID: 1758883
  7. The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.
    J Biol Chem. 1999 Jun 4;274(23):16337-42 PMID: 10347191
  8. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure.
    EMBO J. 1990 May;9(5):1665-72 PMID: 2184035
  9. The CD95(APO-1/Fas) DISC and beyond.
    Cell Death Differ. 2003 Jan;10(1):26-35 PMID: 12655293
  10. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress.
    Science. 2004 May 7;304(5672):843-6 PMID: 15073321
  11. A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen.
    J Biol Chem. 1993 May 25;268(15):10932-7 PMID: 7684370
  12. Three-dimensional structure of a complex between the death domains of Pelle and Tube.
    Cell. 1999 Nov 24;99(5):545-55 PMID: 10589682
  13. The three-dimensional solution structure and dynamic properties of the human FADD death domain.
    J Mol Biol. 2000 Sep 8;302(1):171-88 PMID: 10964568
  14. Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis.
    Nat Genet. 2000 Sep;26(1):122-7 PMID: 10973264
  15. Caspase-2 function in response to DNA damage.
    Biochem Biophys Res Commun. 2005 Jun 10;331(3):859-67 PMID: 15865942
  16. Cell death: critical control points.
    Cell. 2004 Jan 23;116(2):205-19 PMID: 14744432
  17. Apoptosis in the pathogenesis and treatment of disease.
    Science. 1995 Mar 10;267(5203):1456-62 PMID: 7878464
  18. A novel domain within the 55 kd TNF receptor signals cell death.
    Cell. 1993 Sep 10;74(5):845-53 PMID: 8397073
  19. Pathways of apoptosis in lymphocyte development, homeostasis, and disease.
    Cell. 2002 Apr;109 Suppl:S97-107 PMID: 11983156
  20. Crystallography & NMR system: A new software suite for macromolecular structure determination.
    Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21 PMID: 9757107
  21. Improved methods for building protein models in electron density maps and the location of errors in these models.
    Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9 PMID: 2025413
  22. The domains of apoptosis: a genomics perspective.
    Sci STKE. 2004 Jun 29;2004(239):re9 PMID: 15226512
  23. Death receptor signaling.
    J Cell Sci. 2005 Jan 15;118(Pt 2):265-7 PMID: 15654015
  24. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex.
    Immunity. 1996 Apr;4(4):387-96 PMID: 8612133
  25. SOLVE and RESOLVE: automated structure solution, density modification and model building.
    J Synchrotron Radiat. 2004 Jan 1;11(Pt 1):49-52 PMID: 14646132
  26. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor.
    EMBO J. 1995 Nov 15;14(22):5579-88 PMID: 8521815
  27. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex.
    Cell. 1996 Jun 14;85(6):817-27 PMID: 8681377
  28. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules.
    J Mol Graph. 1993 Jun;11(2):134-8, 127-8 PMID: 8347566
  29. RAIDD is a new 'death' adaptor molecule.
    Nature. 1997 Jan 2;385(6611):86-9 PMID: 8985253
  30. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death.
    Cell. 1996 Jun 14;85(6):803-15 PMID: 8681376
  31. Raster3D Version 2.0. A program for photorealistic molecular graphics.
    Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):869-73 PMID: 15299354
  32. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization.
    Science. 2002 Aug 23;297(5585):1352-4 PMID: 12193789
  33. The Fas signaling pathway: more than a paradigm.
    Science. 2002 May 31;296(5573):1635-6 PMID: 12040174
  34. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death.
    Cell. 1994 Sep 9;78(5):739-50 PMID: 8087842
  35. Fire and death: the pyrin domain joins the death-domain superfamily.
    C R Biol. 2004 Dec;327(12):1077-86 PMID: 15656350
  36. Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1.
    Nature. 1999 Jun 10;399(6736):549-57 PMID: 10376594
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
DOI
10.1016/j.jmb.2005.12.082
Published
2006-03-24
Epub
2006-00-11
Pages
358-64
Language
English
Region
England
NLM ID
2985088R
PMCID
PMC2902980
Subset
IM
Grants
NIAID NIH HHS · R01 AI050872 · United States
NIAID NIH HHS · R01 AI050872-06A1 · United States
NIAID NIH HHS · R01 AI-50872 · United States
External Links
PubMed source DOI: 10.1016/j.jmb.2005.12.082 PMC Full Text View journal details
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