Localization of a cryptic binding site for tenascin on fibronectin.

Published

Journal Article

Fibronectin and tenascin are large extracellular matrix proteins that interact with each other and with integrin receptors to regulate cell growth and movement. They are both modular proteins composed of independently folded domains (modules) that are arranged in linear fashion. Fibronectin is a covalent dimer and tenascin is a hexamer. The site on tenascin to which fibronectin binds has been localized to type III modules 3-5. In this study we use surface plasmon resonance to examine the interaction between various fragments of fibronectin and tenascin to further characterize and localize the binding sites. We found that tenascin fragments that contain type III modules 3-5 bind primarily to the N-terminal 29-kDa hep-1/fib-1 domain, which contains the first five type I modules of fibronectin. The dissociation constant, K(d), is approximately 1 microm. The binding site on fibronectin appears to be cryptic in the whole molecule in solution but is exposed on the proteolytic fragments and probably when fibronectin is in the extended conformation.

Full Text

Duke Authors

Cited Authors

  • Ingham, KC; Brew, SA; Erickson, HP

Published Date

  • July 2, 2004

Published In

Volume / Issue

  • 279 / 27

Start / End Page

  • 28132 - 28135

PubMed ID

  • 15123658

Pubmed Central ID

  • 15123658

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M312785200

Language

  • eng

Conference Location

  • United States