Crystal structure of invasin: A bacterial integrin-binding protein

Citation
Za. Hamburger et al., Crystal structure of invasin: A bacterial integrin-binding protein, SCIENCE, 286(5438), 1999, pp. 291-295
Citations number
62
Categorie Soggetti
Multidisciplinary,Multidisciplinary,Multidisciplinary
Journal title
SCIENCE
ISSN journal
00368075 → ACNP
Volume
286
Issue
5438
Year of publication
1999
Pages
291 - 295
Database
ISI
SICI code
0036-8075(19991008)286:5438<291:CSOIAB>2.0.ZU;2-W
Abstract
The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrate s such as fibronectin, The 2.3 angstrom crystal structure of the invasin ex tracellular region reveals five domains that form a 180 angstrom rod with s tructural similarities to tandem fibronectin type III domains. The integrin -binding surfaces of invasin and fibronectin include similarly Located key residues, but in the context of different folds and surface shapes. The str uctures of invasin and fibronectin provide an example of convergent evoluti on, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.