1r17

Structural highlights

Function

SDRG_STAEP Binds to the N-terminus of the B beta-chain of human fibrinogen and thereby interferes with thrombin cleavage and release of fibrinopeptide B, thus interfering with fibrin clot formation. This may hinder host defense against microbial infections.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Fibrinogen binding protein

References

1. ↑ Davis SL, Gurusiddappa S, McCrea KW, Perkins S, Hook M. SdrG, a fibrinogen-binding bacterial adhesin of the microbial surface components recognizing adhesive matrix molecules subfamily from Staphylococcus epidermidis, targets the thrombin cleavage site in the Bbeta chain. J Biol Chem. 2001 Jul 27;276(30):27799-805. Epub 2001 May 22. PMID:11371571 doi:http://dx.doi.org/10.1074/jbc.M103873200