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The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist.

Abstract:

An important goal of structural studies of modular proteins is to determine the inter-module orientation, which often influences biological function. The N-terminal domain of human fibronectin (Fn) is composed of a string of five type 1 modules (F1). Despite their small size, to date F1 modules have proved intractable to X-ray structure solution, although there are several NMR structures available. Here, we present the first structures (two X-ray models and an NMR-derived model) of the (2)F1(...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2007.02.061

Authors


Rudiño-Piñera, E More by this author
Ravelli, RB More by this author
Sheldrick, GM More by this author
Korostelev, VV More by this author
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Journal:
Journal of molecular biology
Volume:
368
Issue:
3
Pages:
833-844
Publication date:
2007-05-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:195f930c-fba7-405b-879e-6b99bb66eeec
Source identifiers:
100259
Local pid:
pubs:100259

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