Related Experiment Video
Updated: Jun 12, 2026

Observing and Quantifying Fibroblast-mediated Fibrin Gel Compaction
Published on: January 16, 2014
Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding
Marc Graille1, Maurice Pagano, Thierry Rose
1IBBMC, Université Paris 11, IFR115, CNRS UMR8619, Orsay Cedex F-91405, France. marc.graille@u-psud.fr <marc.graille@u-psud.fr>
Abstract:
Fibronectin is a modular extracellular matrix protein involved in cell adhesion, cell motility, wound healing, and maintenance of cell morphology. It is composed of multiple repeats of three distinct modules: F(I), F(II), and F(III). Various combinations of these modules create fragments able to interact with different constituents of the extracellular matrix. Here, we present the 2.5-A resolution crystal structure of its 45-kDa gelatin-binding domain (GBD; 6F(I)-1F(II)-2F(II)-7F(I)-8F(I)-9F(I)), which also corresponds to the C-terminal half of the migration stimulating factor, a Fn splice variant expressed in human breast cancers. GBD forms a very compact zinc-mediated homodimer, in stark contrast with previous structures of fibronectin fragments. Most remarkably, 8F(I) no longer adopts the canonical F(I) fold but is composed of two long strands that associate with 7F(I) and 9F(I) into a large beta-sheet superdomain. Binding studies in solution confirmed that Zn induces conformational rearrangements and causes loss of binding of Fn-GBD to high-affinity collagen peptides. These data suggest the Zn may play a regulatory role for the cellular functions of fibronectin.
Related Concept Videos
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Fibronectins Connect Cells with ECM
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Fibril-associated Collagen
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Type IV Collagen of Basal Lamina
A type IV collagen molecule has six alpha chains which can exist in...
Cell-matrix's Response to Mechanical Forces
Anchoring junctions mechanically attach a cell to the...
Intracellular Signaling Affects Focal Adhesions
Some...
