3GXE

Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair

Summary for 3GXE

• Entry DOI: 10.2210/pdb3gxe/pdb
• Related: 3EJH
• Descriptor: Fibronectin, Collagen alpha-1(I) chain, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: protein-peptide complex, cell adhesion
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 26879.57

Authors

Sladek, B.,Campbell, I.D.,Vakonakis, I. (deposition date: 2009-04-02, release date: 2010-04-07, Last modification date: 2023-11-22)

Primary citation

Erat, M.C.,Sladek, B.,Campbell, I.D.,Vakonakis, I.
Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode
J.Biol.Chem., 288:17441-17450, 2013

PubMed Abstract: Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abundant and crucial tissue components, has not been well characterized on a structural level. Here, we analyzed the four interactions formed between epitopes of collagen type I and the collagen-binding fragment (gelatin-binding domain (GBD)) of human FN using solution NMR, fluorescence, and small angle x-ray scattering methods. Collagen association with FN modules (8-9)FnI occurs through a conserved structural mechanism but exhibits a 400-fold disparity in affinity between collagen sites. This disparity is reduced in the full-length GBD, as (6)FnI(1-2)FnII(7)FnI binds a specific collagen epitope next to the weakest (8-9)FnI-binding site. The cooperative engagement of all GBD modules with collagen results in four broadly equipotent FN-collagen interaction sites. Collagen association stabilizes a distinct monomeric GBD conformation in solution, giving further evidence to the view that FN fragments form well defined functional and structural units.

PubMed: 23653354
DOI: 10.1074/jbc.M113.469841

Experimental method

X-RAY DIFFRACTION (2.6 Å)