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Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode.

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...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m113.469841

Authors


Campbell, ID More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
The Journal of biological chemistry
Volume:
288
Issue:
24
Pages:
17441-17450
Publication date:
2013-06-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:01bdc3ba-bf49-4742-b7b9-c1d989c7d9fe
Source identifiers:
401474
Local pid:
pubs:401474

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