Structural highlights
Publication Abstract from PubMed
Bacterial pathogens secrete effectors into their hosts that subvert host defenses and redirect host processes. EspG is a type three secretion effector with a disputed function that is found in enteropathogenic Escherichia coli. Here we show that EspG is structurally similar to VirA, a Shigella virulence factor; EspG has a large, conserved pocket on its surface; EspG binds directly to the amino-terminal inhibitory domain of human p21-activated kinase (PAK); and mutations to conserved residues in the surface pocket disrupt the interaction with PAK.
Structural and Functional Studies Indicate That the EPEC Effector, EspG, Directly Binds p21-Activated Kinase.,Germane KL, Spiller BW Biochemistry. 2011 Feb 15;50(6):917-9. Epub 2011 Jan 24. PMID:21235237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Germane KL, Spiller BW. Structural and Functional Studies Indicate That the EPEC Effector, EspG, Directly Binds p21-Activated Kinase. Biochemistry. 2011 Feb 15;50(6):917-9. Epub 2011 Jan 24. PMID:21235237 doi:10.1021/bi1020138
