Structural highlights
Publication Abstract from PubMed
We have observed that the extracellular domain of T beta RI 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 T beta RI 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 T beta RI, T beta RII and TGF beta during ligand recognition and signal transduction.
Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template.,Jokiranta TS, Tissari J, Teleman O, Meri S FEBS Lett. 1995 Nov 27;376(1-2):31-6. PMID:8521960[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jokiranta TS, Tissari J, Teleman O, Meri S. Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template. FEBS Lett. 1995 Nov 27;376(1-2):31-6. PMID:8521960