Structural highlights
Function
PKND_MYCTU Key microbial factor required for central nervous system tuberculosis. Required for invasion of host brain endothelia, but not macrophages, lung epithelia or other endothelia. Phosphorylates the anti-anti-sigma factor homolog Rv0516c, which inhibits binding of Rv0516c to Rv2638, another anti-anti-sigma factor. Can also phosphorylate the FHA domain of Rv1747.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Grundner C, Gay LM, Alber T. Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains. Protein Sci. 2005 Jul;14(7):1918-21. PMID:15987910 doi:http://dx.doi.org/10.1110/ps.051413405
- ↑ Greenstein AE, Echols N, Lombana TN, King DS, Alber T. Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis. J Biol Chem. 2007 Apr 13;282(15):11427-35. Epub 2007 Jan 22. PMID:17242402 doi:http://dx.doi.org/10.1074/jbc.M610193200
- ↑ Greenstein AE, MacGurn JA, Baer CE, Falick AM, Cox JS, Alber T. M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. PLoS Pathog. 2007 Apr;3(4):e49. PMID:17411339 doi:http://dx.doi.org/10.1371/journal.ppat.0030049