The ligand binding domain of the epidermal growth factor receptor is not required for receptor dimerization.

Published

Journal Article

To examine the role of the ligand binding domain of epidermal growth factor receptor in its dimerization, we studied the dimerization of a truncated form of the receptor that resembles v-erbB in that it lacks a ligand binding domain. Receptor dimerization was determined by sedimentation analysis on sucrose density gradients at different concentrations of Triton X-100. At high concentrations of Triton X-100 (0.2%), the truncated receptor occurred as a monomer and displayed low basal autophosphorylation. By contrast, at low concentrations of Triton X-100 (0.01%), it existed as a dimer and exhibited high basal autophosphorylation. The ability of the truncated receptor to dimerize indicates that the ligand binding domain of the epidermal growth factor receptor is not required for receptor dimerization.

Full Text

Duke Authors

Cited Authors

  • Kwatra, MM; Bigner, DD; Cohn, JA

Published Date

  • March 16, 1992

Published In

Volume / Issue

  • 1134 / 2

Start / End Page

  • 178 - 181

PubMed ID

  • 1554751

Pubmed Central ID

  • 1554751

International Standard Serial Number (ISSN)

  • 0006-3002

Digital Object Identifier (DOI)

  • 10.1016/0167-4889(92)90042-a

Language

  • eng

Conference Location

  • Netherlands