Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template.
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.
Jokiranta
T S
TS
Department of Bacteriology, Haartman Institute, University of Helsinki, Finland.
Tissari
J
J
Teleman
O
O
Meri
S
S
D000595:Amino Acid Sequence; D018957:CD59 Antigens / Q000737:chemistry*; D015938:Complement Membrane Attack Complex / Q000037:antagonists & inhibitors; D003196:Computer Graphics; D003545:Cysteine / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D018125:Receptors, Transforming Growth Factor beta / Q000737:chemistry*; D016415:Sequence Alignment
D018957:CD59 Antigens; D015938:Complement Membrane Attack Complex; D018125:Receptors, Transforming Growth Factor beta; D003545:Cysteine