Abstract
We have observed that the extracellular domain of TβRI and protectin (CD59), an inhibitor of the membrane attack complex of complement, share structural features, a distinct spacing of ten cysteines and a C‐terminal ‘Cys‐box’. Based on these common features and the recently determined NMR‐structure of protectin, a three‐dimensional model for the extracellular domain of TβRI was constructed. After energy minimization and molecular dynamics simulation, a structure with four extending fingers (pes quattvordigitorum) and two clusters of charged residues was obtained. This model provides a view to the understanding of interactions between TβRI, TβRII and TGFβ during ligand recognition and signal transduction.
Original language | English |
---|---|
Pages (from-to) | 31-36 |
Journal | FEBS Letters |
Volume | 376 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1995 |
MoE publication type | A1 Journal article-refereed |
Keywords
- molecular modelling
- chemical modelling