Journal Article

PHPPUBDB-26532

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural Analysis of Collagen Type I Interactions with Human Fibronectin Reveals a Cooperative Binding Mode

Erat, M. C. (Corresponding author)>Extern* ; Sladek, B. ; Campbell, I. D. ; Vakonakis, I. (Corresponding author) ; DESY

2013
Soc. Bethesda, Md.

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Please use a persistent id in citations: doi:10.1074/jbc.M113.469841  doi:10.3204/PHPPUBDB-26532

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.

Note: © by The American Society for Biochemistry and Molecular Biology, Inc.

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Contributing Institute(s):

1. DOOR-User (DOOR)

Research Program(s):

1. DORIS Beamline D1.2 (POF1-550) (POF1-550)

Experiment(s):

1. DORIS Beamline D1.2 (DORIS III)

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