Crystal structure of the soluble human 55 kd TNF receptor-human TNFbeta complex: implications for TNF receptor activation
Article Abstract:
A 2.85 Angstrom-resolution crystal structure of the 55 kd tumor necrosis factor (TNF)-human TNFbeta complex was obtained using the heavy atom multiple isomorphous replacement method combined with solvent flattening. Structural analysis of the molecule indicates a complex comprising of three receptor molecules symmetrically bound to one TNFbeta trimer. The receptor fragment is an end to end assembly of four similar folding domains that binds in the groove between two adjacent TNFbeta subunits. It is propsed that this structure reflects the activation state of the TNF receptor at the cell surface and provides a model for TNF signal generation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
User Contributions:
Comment about this article or add new information about this topic:
The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
Article Abstract:
The cytoplasmic C-terminus of Epstein-Barr virus (EBV) latent infection membrane protein (LMP1) associates with a human protein, LMP1-associated protein 1 (LAP1), and with the EB 16 protein. LAP1 is homologous to tumor necrosis factor receptor (TNFR)-associated factor 2, while the EB 16 protein, is homologous to human TNFR-associated protein. Colocalization of EB16 and LAP1 proteins occurs due to LMP1 expression in the LMP1 clusters in the plasma membranes of lymphoblasts. The binding between LMP1 and p80 TNFR, and lymphotoxin-beta receptor and CD40 indicates their contribution to cellular signaling pathways.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor
Article Abstract:
The transmembrane form of tumor necrosis factor (mTNF) activates the 80 kDa tumor necrosis factor receptor (TNFR(sub 80)) and changes the cell's phenotype. These changes include making TNF-resistant cells sensitive to TNF. The stimulatory activity of mTNF is stronger than that of soluble TNF. Cooperativity between the two receptors increases the cellular response to TNF as mTNF also activates TNFR(sub 60).
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Crystal structure of the cys2 activator-binding domain of protein kinase C-delta in complex with phorbol ester
- Abstracts: The 2.8 Angstrom crystal structure of visual arrestin: a model for arrestin's regulation. Arrestin binding determines the rate of inactivation of the G protein-coupled receptor rhodopsin in vivo
- Abstracts: NSF-independent fusion mechanisms. Calcium mobilization is required for nuclear vesicle fusion in vitro: implications for membrane traffic and IP3 receptor function
- Abstracts: Purification and characterization of the soluble methane monooxygenase of the type II methanotrophic bacterium Methylocystis sp. strain WI 14
- Abstracts: Alternative function of the electron transport system in Azotobacter vinelandii: removal of excess reductant by the cytochrome d pathway