1DDF

FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1DDF

• Entry DOI: 10.2210/pdb1ddf/pdb
• Descriptor: FAS (1 entity in total)
• Functional Keywords: death domain, apoptosis, receptor, glycoprotein, transmembrane
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted. Isoform 4: Secreted. Isoform 5: Secreted. Isoform 6: Secreted: P25445
• Total number of polymer chains: 1
• Total formula weight: 14535.48

Authors

Huang, B.,Eberstadt, M.,Olejniczak, E.,Meadows, R.P.,Fesik, S. (deposition date: 1996-11-08, release date: 1997-11-12, Last modification date: 2024-05-22)

Primary citation

Huang, B.,Eberstadt, M.,Olejniczak, E.T.,Meadows, R.P.,Fesik, S.W.
NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain.
Nature, 384:638-641, 1996

PubMed Abstract: Programmed cell death (apoptosis) mediated by the cytokine receptor Fas is critical for the removal of autoreactive T cells, the mechanism of immune privilege, and for maintenance of immune-system homeostasis. Signalling of programmed cell death involves the self-association of a conserved cytoplasmic region of Fas called the death domain and interaction with another death-domain-containing protein, FADD (also known as MORT1). Although death domains are found in several proteins, their three-dimensional structure and the manner in which they interact is unknown. Here we describe the solution structure of the Fas death domain, as determined by NMR spectroscopy. The structure consists of six antiparallel, amphipathic alpha-helices arranged in a novel fold. From the structure and from site-directed mutagenesis, we have identified the region of the death domain involved in self-association and binding to the downstream signalling partner FADD.

PubMed: 8967952
DOI: 10.1038/384638a0

Experimental method

SOLUTION NMR