1DDF

FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

1DDF の概要

• エントリーDOI: 10.2210/pdb1ddf/pdb
• 分子名称: FAS (1 entity in total)
• 機能のキーワード: death domain, apoptosis, receptor, glycoprotein, transmembrane
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14535.48

構造登録者

Huang, B.,Eberstadt, M.,Olejniczak, E.,Meadows, R.P.,Fesik, S. (登録日: 1996-11-08, 公開日: 1997-11-12, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

SOLUTION NMR