CONSERVATIVE HYDROPHOBIC INTERDOMAIN CONTACTS OF IFN-GAMMA REMAIN IN P17 MATRIX PROTEIN OF HIV-1

A constructed scheme of the surface layers containing helices C, D, an d E' of various polypeptide chains which participate in the interdomai n contacts in IFN-gamma demonstrated two sites of localization of the conservative hydrophobic amino acids. Pin analogous scheme of the inte raction of helices B, C, and D in the p17 matrix protein of HIV-1 show ed that the majority of the hydrophobic positions are similar. These d ata confirm the structural similarity between p17 and IFN-gamma.