title: A role of disordered domains in regulating protein oligomerization and stability.
abstract: Intrinsically disordered proteins (IDPs) or regions (IDRs) in proteins hold many functions but their biological roles are still not fully understood. Here we describe a new role of such regions. Using the HIV-1 Rev protein, we show that disordered domains have a role in maintaining the correct oligomeric state and the thermodynamic stability of proteins.
authors: Institute of Chemistry, The Hebrew University of Jerusalem, The Edmond J. Safra Campus, Givat Ram 91904, Jerusalem, Israel. assaf.friedler@mail.huji.ac.il.
authors: Ofrah
authors: O
authors: Faust
authors: Lavi
authors: L
authors: Bigman
authors: Assaf
authors: A
authors: Friedler
mesh_terms: D015497:HIV-1 / Q000378:metabolism; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism; D055503:Protein Multimerization; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D013816:Thermodynamics; D054321:rev Gene Products, Human Immunodeficiency Virus / Q000737:chemistry / Q000378:metabolism
chemical_list: D064267:Intrinsically Disordered Proteins; D054321:rev Gene Products, Human Immunodeficiency Virus; C514860:rev protein, Human Immunodeficiency Virus-1