Abstract:
: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.
journal_name
Celljournal_title
Cellauthors
Leahy DJ,Aukhil I,Erickson HPdoi
10.1016/s0092-8674(00)81002-8subject
Has Abstractpub_date
1996-01-12 00:00:00pages
155-64issue
1eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81002-8journal_volume
84pub_type
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