The Fas–FADD death domain complex structure unravels signalling by receptor clustering

Fiona L. Scott, Boguslaw Stec, Cristina Pop, Małgorzata K. Dobaczewska, JeongEun J. Lee, Edward Monosov, Howard Robinson, Guy S. Salvesen, Robert Schwarzenbacher () and Stefan J. Riedl ()
Additional contact information
Fiona L. Scott: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
Boguslaw Stec: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
Cristina Pop: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
Małgorzata K. Dobaczewska: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
JeongEun J. Lee: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
Edward Monosov: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
Howard Robinson: Brookhaven National Laboratory, Upton, New York 11973, USA
Guy S. Salvesen: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
Robert Schwarzenbacher: University of Salzburg
Stefan J. Riedl: Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA

Nature, 2009, vol. 457, issue 7232, 1019-1022

Abstract: The complexities of cell death The crystal structure of a complex between the cell surface receptor protein Fas and the Fas-associated death domain (FADD) protein - a central feature of the so-called death-inducing signalling complex of apoptosis-inducing cellular receptors - has been determined at 2.7 Å resolution. The structure reveals a previously unknown type of death domain interaction that allows four FADD and four Fas proteins to aggregate in the one complex. Surprisingly, a conformational change opens up the Fas death domain, which creates binding surfaces for FADD as well as Fas-Fas 'bridging' interactions. Only when a sufficient number of Fas molecules are in close proximity - as is the case when Fas ligand binds - can the open form of Fas be stabilized.

Date: 2009
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DOI: 10.1038/nature07606

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