2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region

Daniel J. Leahy, Ikramuddin Aukhil, Harold P. Erickson

Research output: Contribution to journalArticlepeer-review

Abstract

We have determined the 2.0 Å crystal structure of a fragment of human fibronectin encompassing the seventh through the RGD-containing tenth type III repeats (FN7-10). The structure reveals an extended rod-like molecule with a long axis of ∼140 Å and highly variable relationships between adjacent domains. An unusually small rotation between domains 9 and 10 creates a distinctive binding site, in which the RGD loop from domain 10 and the synergy region from domain 9 are on the same face of FN7-10 and thus easily accessible to a single integrin molecule. The cell-binding RGD loop is well-ordered in this structure and extends ∼10 Å away from the FN7-10 core.

Original languageEnglish (US)
Pages (from-to)155-164
Number of pages10
JournalCell
Volume84
Issue number1
DOIs
StatePublished - Jan 12 1996

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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