2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.
We have determined the 2.0 A 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 approximately 140 A 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 approximately 10 A away from the FN7-10 core.
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21218, USA.
D J
DJ
Leahy
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Aukhil
H P
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Erickson
D000595:Amino Acid Sequence; D003461:Crystallography; D005353:Fibronectins / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D007091:Image Processing, Computer-Assisted; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation
D005353:Fibronectins; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid