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 language | English (US) |
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Pages (from-to) | 155-164 |
Number of pages | 10 |
Journal | Cell |
Volume | 84 |
Issue number | 1 |
DOIs | |
State | Published - Jan 12 1996 |
Externally published | Yes |
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology