TY  - JOUR
AU  - Erat, M. C.
AU  - Sladek, B.
AU  - Campbell, I. D.
AU  - Vakonakis, I.
AU  - DESY
TI  - Structural Analysis of Collagen Type I Interactions with Human Fibronectin Reveals a Cooperative Binding Mode
JO  - The journal of biological chemistry
VL  - 288
IS  - 24
SN  - 0021-9258
CY  - Bethesda, Md.
PB  - Soc.
M1  - PHPPUBDB-26532
SP  - 17441 - 17450
PY  - 2013
N1  - © by The American Society for Biochemistry and Molecular Biology, Inc.
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000320380600036
C6  - pmid:23653354
DO  - DOI:10.1074/jbc.M113.469841
UR  - https://bib-pubdb1.desy.de/record/151882
ER  -