A bacterial cell moves toward a beneficial environment and away from a hostile one in the process known as chemotaxis. This chemotatic behavior is mediated by the signaling complex which consists of a chemoreceptor, a histidine kinase CheA and a coupling protein CheW. The signaling complex regulates kinase activity, in turn controlling the rotational bias of flagella. The high-resolution structures of individual chemotaxis proteins involved in the signaling complex have been solved either by X-ray crystallography or nuclear magnetic resonance (NMR), yet the interaction between chemoreceptors and CheW is still unclear. Here we used NMR to characterize the interaction modes of chemoreceptor, CheA and CheW from Thermotoga maritima. We find that the chemoreceptor binding surface is located near the highly conserved tip region of the N-terminal helix of the receptor. The receptor interaction surfaces of CheA and CheW are located in similar hydrophobic patches located about 55A apart. This suggests one receptor dimer is required to occupy on each binding site of CheA and CheW and is antiparallel to P3 domain of CheA. Our NMR data and previous studies suggest that a rearrangement of each subunit of CheA dimer is important for kinase activation. Our results provide direct observation of receptor-CheA-CheW interaction and have implications for the kinase activation in bacterial chemotaxis.