Structural highlights
Function
[INVA_YERPS] Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrates such as fibronectin. The 2.3 angstrom crystal structure of the invasin extracellular region reveals five domains that form a 180 angstrom rod with structural 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 structures of invasin and fibronectin provide an example of convergent evolution, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.
Crystal structure of invasin: a bacterial integrin-binding protein.,Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ Science. 1999 Oct 8;286(5438):291-5. PMID:10514372[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ. Crystal structure of invasin: a bacterial integrin-binding protein. Science. 1999 Oct 8;286(5438):291-5. PMID:10514372
