Work

2.0 Å Crystal Structure of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop and Synergy Region

Year: 1996

Type: article

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.

Source: Cell

DOI: 10.1016/s0092-8674(00)81002-8

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

Institutions: Johns Hopkins University, Johns Hopkins Medicine, University of North Carolina at Chapel Hill, Duke Medical Center

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $11,400

Funders: National Heart, Lung, and Blood Institute, National Cancer Institute, National Institute of Dental and Craniofacial Research