Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template

Sakari Jokiranta (Corresponding Author), Jorma Tissari, Olle Teleman, Seppo Meri

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)31-36
JournalFEBS Letters
Volume376
Issue number1-2
DOIs
Publication statusPublished - 1995
MoE publication typeA1 Journal article-refereed

Fingerprint

CD59 Antigens
Molecular modeling
Complement Membrane Attack Complex
Signal transduction
Molecular Dynamics Simulation
Fingers
Cysteine
Molecular dynamics
Signal Transduction
Ligands
Computer simulation
TGF-beta type I receptor

Keywords

  • molecular modelling
  • chemical modelling

Cite this

Jokiranta, Sakari ; Tissari, Jorma ; Teleman, Olle ; Meri, Seppo. / Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template. In: FEBS Letters. 1995 ; Vol. 376, No. 1-2. pp. 31-36.
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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 journalArticleScientificpeer-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

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JF - FEBS Letters

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