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, and E' of various polypeptide chains which participate in the interdomain contacts in IFN-gamma demonstrated two sites of localization of the conservative hydrophobic amino acids. An analogous scheme of the interaction of helices B, C, and D in the p17 matrix protein of HIV-1 showed that the majority of the hydrophobic positions are similar. These data confirm the structural similarity between p17 and IFN-gamma.
Denesyuk
A I
AI
Finnish-Russian Joint Biotechnology Laboratory, University of Turku, Finland.
Matthews
S
S
Zav'yalov
V P
VP
Korpela
T
T
D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D016208:Databases, Factual; D015683:Gene Products, gag / Q000737:chemistry* / Q000276:immunology*; D015488:HIV Antigens / Q000737:chemistry* / Q000276:immunology*; D015497:HIV-1 / Q000502:physiology*; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry* / Q000378:metabolism; D008961:Models, Structural; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000276:immunology*; D014764:Viral Proteins; D054301:gag Gene Products, Human Immunodeficiency Virus
D015683:Gene Products, gag; D015488:HIV Antigens; D014763:Viral Matrix Proteins; D014764:Viral Proteins; D054301:gag Gene Products, Human Immunodeficiency Virus; C054858:p17 protein, Human Immunodeficiency Virus Type 1; D007371:Interferon-gamma