Evidence for the "dock, lock, and latch" ligand binding mechanism of the staphylococcal microbial surface component recognizing adhesive matrix molecules (MSCRAMM) SdrG.

@article{Bowden2008EvidenceFT,
  title={Evidence for the "dock, lock, and latch" ligand binding mechanism of the staphylococcal microbial surface component recognizing adhesive matrix molecules (MSCRAMM) SdrG.},
  author={Maria Gabriela Bowden and Alejandro P Heuck and Karthe Ponnuraj and Elena Kolosova and Damon Choe and Sivashankarappa Gurusiddappa and Sthanam V. L. Narayana and Arthur E. Johnson and Magnus H{\"o}{\"o}k},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 1},
  pages={638-47}
}
Staphylococcus epidermidis is an opportunistic pathogen and a major cause of foreign body infections. The S. epidermidis fibrinogen (Fg)-binding adhesin SdrG is necessary and sufficient for the attachment of this pathogen to Fg-coated materials. Based largely on structural analyses of the ligand binding domain of SdrG as an apo-protein and in complex with a Fg-like peptide, we proposed that SdrG follows a "dock, lock, and latch" mechanism to bind to Fg. This binding mechanism involves the… CONTINUE READING

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