Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Jokiranta TS,Tissari J,Teleman O,Meri Sdoi
10.1016/0014-5793(95)01239-7subject
Has Abstractpub_date
1995-11-27 00:00:00pages
31-6issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(95)01239-7journal_volume
376pub_type
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