TY - JOUR AU - Simpkin, Adam J. AU - Rigden, Daniel J. PY - 2016 DA - 2016/07/13 TI - GP0.4 from bacteriophage T7: in silico characterisation of its structure and interaction with E. coli FtsZ JO - BMC Research Notes SP - 343 VL - 9 IS - 1 AB - Proteins produced by bacteriophages can have potent antimicrobial activity. The study of phage-host interactions can therefore inform small molecule drug discovery by revealing and characterising new drug targets. Here we characterise in silico the predicted interaction of gene protein 0.4 (GP0.4) from the Escherichia coli (E. coli) phage T7 with E. coli filamenting temperature-sensitive mutant Z division protein (FtsZ). FtsZ is a tubulin homolog which plays a key role in bacterial cell division and that has been proposed as a drug target. SN - 1756-0500 UR - https://doi.org/10.1186/s13104-016-2149-5 DO - 10.1186/s13104-016-2149-5 ID - Simpkin2016 ER -