📣 Help Shape the Future of UKRI's Gateway to Research (GtR)

We're improving UKRI's Gateway to Research and are seeking your input! If you would be interested in being interviewed about the improvements we're making and to have your say about how we can make GtR more user-friendly, impactful, and effective for the Research and Innovation community, please email gateway@ukri.org.

The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules. (2010)

First Author: Atkin KE

Attributed to: Structural studies of the full fibronectin-binding site of pathogenic bacteria-extending and characterizing the tandem beta-zipper funded by BBSRC

Abstract

No abstract provided

Bibliographic Information

Digital Object Identifier: http://dx.doi.org/10.1074/jbc.m110.156935

PubMed Identifier: 20843804

Publication URI: http://europepmc.org/abstract/MED/20843804

Type: Journal Article/Review

Volume: 285

Parent Publication: The Journal of biological chemistry

Issue: 47

ISSN: 0021-9258