1E41

Death domain from human FADD/MORT1

1E41 の概要

• エントリーDOI: 10.2210/pdb1e41/pdb
• 関連するPDBエントリー: 1A1W 1A1Z 1E3Y
• 分子名称: FADD PROTEIN (1 entity in total)
• 機能のキーワード: apoptosis, death domain, adapter molecule, fas receptor death inducing signalling complex
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11870.37

構造登録者

Driscoll, P.C.,Berglund, H.,Olerenshaw, D.,McDonald, N.Q. (登録日: 2000-06-27, 公開日: 2000-11-06, 最終更新日: 2024-05-15)

主引用文献

Berglund, H.,Olerenshaw, D.,Sankar, A.,Federwisch, M.,Mcdonald, N.Q.,Driscoll, P.C.
The Three-Dimensional Solution Structure and Dynamic Properties of the Human Fadd Death Domain
J.Mol.Biol., 302:171-, 2000

PubMed Abstract: FADD (also known as MORT-1) is an essential adapter protein that couples the transmembrane receptors Fas (CD95) and tumor necrosis factor receptor-1 (TNF-R1) to intracellular cysteine proteases known as caspases, which propagate and execute the programmed cell death-inducing signal triggered by Fas ligand (FasL, CD95L) and TNF. FADD contains 208 amino acid residues, and comprises two functionally and structurally distinct domains: an N-terminal death effector domain (DED) that promotes activation of the downstream proteolytic cascade through binding of the DED domains of procaspase-8; and a C-terminal death domain (DD). FADD-DD provides the site of FADD recruitment to death receptor complexes at the plasma membrane by, for example, interaction with the Fas receptor cytoplasmic death domain (Fas-DD), or binding of the TNF-R1 adapter molecule TRADD. We have determined the three-dimensional solution structure and characterised the internal polypeptide dynamics of human FADD-DD using heteronuclear NMR spectroscopy of (15)N and (13)C,(15)N-labelled samples. The structure comprises six alpha-helices joined by short loops and displays overall similarity to the death domain of the Fas receptor. The analysis of the dynamic properties reveals no evidence of contiguous stretches of polypeptide chain with increased internal motion, except at the extreme chain termini. A pattern of increased rates of amide proton solvent exchange in the alpha3 helix correlates with a higher degree of solvent exposure for this secondary structure element. The properties of the FADD-DD structure are discussed with respect to previously reported mutagenesis data and emerging models for FasL-induced FADD recruitment to Fas and caspase-8 activation.

PubMed: 10964568
DOI: 10.1006/JMBI.2000.4011

実験手法

SOLUTION NMR