Abstract
| 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 |
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Keywords
- molecular modelling
- chemical modelling
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Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template. / Jokiranta, Sakari (Corresponding Author); Tissari, Jorma; Teleman, Olle; Meri, Seppo.
In: FEBS Letters, Vol. 376, No. 1-2, 1995, p. 31-36.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template
AU - Jokiranta, Sakari
AU - Tissari, Jorma
AU - Teleman, Olle
AU - Meri, Seppo
PY - 1995
Y1 - 1995
N2 - 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.
AB - 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.
KW - molecular modelling
KW - chemical modelling
U2 - 10.1016/0014-5793(95)01239-7
DO - 10.1016/0014-5793(95)01239-7
M3 - Article
VL - 376
SP - 31
EP - 36
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -