1cwv
CRYSTAL STRUCTURE OF INVASIN: A BACTERIAL INTEGRIN-BINDING PROTEIN
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1CWV is a Single protein structure of sequence from Yersinia pseudotuberculosis. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Mar 30 19:30:12 2008