Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Prediction of the three-dimensional structure of the human Fas receptor by comparative molecular modeling.

Literature DB >> 9139110

Prediction of the three-dimensional structure of the human Fas receptor by comparative molecular modeling.

Abstract

The Fas antigen, a cell surface receptor belonging to the tumor necrosis factor receptor (TNFR) superfamily, triggers programmed cell death (apoptosis) in the immune system. The three-dimensional structure of Fas and molecular details of the interaction between Fas and its ligand are currently unknown. A three-dimensional model of the Fas extracellular region was generated by comparative modeling. Inverse folding analysis suggested good sequence-structure compatibility of the model and thus reasonable accuracy. The model was analyzed in the light of information provided by studies on TNFR and CD40, another member of the TNFR family, and the Fas ligand binding site was predicted.

Entities: Gene Species

Mesh：

Substances：

Year: 1997 PMID： 9139110 DOI： 10.1023/a:1008011024584

Source DB: PubMed Journal: J Comput Aided Mol Des ISSN： 0920-654X Impact factor: 3.686

18 in total

Prediction of the three-dimensional structure of the human Fas receptor by comparative molecular modeling.

1. Schematic drawings of protein structures.

2. Progressive sequence alignment as a prerequisite to correct phylogenetic trees.

3. Unraveling function in the TNF ligand and receptor families.

4. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features.

Review 5. Immune regulation by CD40 and its ligand GP39.

6. The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis.

7. Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome.

8. 2 A crystal structure of an extracellular fragment of human CD40 ligand.

9. Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor.

10. The mouse Fas-ligand gene is mutated in gld mice and is part of a TNF family gene cluster.

1. Analysis of Fas-ligand interactions using a molecular model of the receptor-ligand interface.

2. Identification of amino acid residues important for ligand binding to Fas.