NOE-derived conformation of GRGDSP cell adhesion recognition site in the presence of SDS micelles and integrin receptor GPIIB/IIIA

Kevin H. Mayo, Francis Fan, Mary Pat Beavers, Annette Eckardt, Patricia Keane, William J. Hoekstra, Patricia Andrade-Gordon

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

The tripeptide RGD is well known for its role in integrin receptor-mediated cell-cell surface adhesion. Here, NMR and transferred NOE studies have been done with the fibrinogen/fibronectin-derived hexapeptide GRGDSP in the presence of sodium dodecyl sulfate (SDS) and purified platelet glycoprotein integrin receptor GPIIb/IIIa. In the presence of SDS and absence of receptor, GRGDSP gives NOE-based distance geometry-generated structures characteristic of two 'nested' β-turns centered at RG and GD. In the presence of integrin GPIIb/IIIa, GRGDSP resonances are chemically shifted and broadened consistent with a dynamic equilibrium between free and receptor 'bound' peptide. NOEs characteristic of the nested β-turns are either absent or weaker indicating a significant conformational change in GRGDSP in the receptor bound state. GRGDSP appears to bind the receptor in a more extended backbone conformation which positions aspartic acid and arginine residues spatially close for potential electrostatic interactions.

Original languageEnglish (US)
Pages (from-to)95-102
Number of pages8
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1296
Issue number1
DOIs
StatePublished - Aug 15 1996

Keywords

  • Binding
  • Intgrin
  • NMR
  • Peptide
  • Receptor
  • Structure

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