Molecular dynamics simulation of egf and tgf-α: Conformation and receptor binding properties

Sándor Lovas, Richard F. Murphy

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Three 1 ns-long molecular dynamics (MD) simulations were performed on murine epidermal growth factor (mEGF), human epidermal growth factor (hEGF) and human transforming growth factor-alpha (hTGF-α) to obtain further information about their conformational properties. The initial structures were taken based on NMR spectroscopy data and were energy-minimized before MD simulations. No major conformational transitions were observed during simulations. Domain movements, predictable from the mitten model of EGF, were observed only in the simulation of hTGF-α and could account for its different receptor binding properties. Inter-domain interactions, not revealed by the NMR data, were observed between aromatic side-chains for each of the polypeptides and seem to stabilize the conformation necessary for binding.

Original languageEnglish
Pages (from-to)543-550
Number of pages8
JournalJournal of Molecular Structure: THEOCHEM
Volume398-399
StatePublished - Jun 30 1997

Fingerprint

Molecular Dynamics Simulation
Epidermal Growth Factor
Conformations
Molecular dynamics
molecular dynamics
Computer simulation
simulation
Polypeptides
nuclear magnetic resonance
Nuclear magnetic resonance spectroscopy
polypeptides
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Peptides
spectroscopy
human TGFA protein
Intercellular Signaling Peptides and Proteins
interactions
energy

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Computational Theory and Mathematics
  • Atomic and Molecular Physics, and Optics

Cite this

Molecular dynamics simulation of egf and tgf-α : Conformation and receptor binding properties. / Lovas, Sándor; Murphy, Richard F.

In: Journal of Molecular Structure: THEOCHEM, Vol. 398-399, 30.06.1997, p. 543-550.

Research output: Contribution to journalArticle

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