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Extracellular domain of type I receptor for transforming growth factor‐β: molecular modelling using protectin (CD59) as a template
Author(s) -
Jokiranta T.Sakari,
Tissari Jorma,
Teleman Olle,
Meri Seppo
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01239-7
Subject(s) - extracellular , transforming growth factor , domain (mathematical analysis) , chemistry , microbiology and biotechnology , cd59 , growth factor , receptor , biology , biochemistry , immunology , complement system , mathematics , antibody , mathematical analysis
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.