Crystal structure of a human Mob1 protein: toward understanding Mob-regulated cell cycle pathways.

摘要: The Mob protein family comprises a group of highly conserved eukaryotic proteins whose founding member functions in the mitotic exit network. At molecular level, act as kinase-activating subunits. We cloned human Mob1 member, Mob1A, and determined its three-dimensional structure by X-ray crystallography. core Mob1A consists four-helix bundle that is stabilized bound zinc atom. N-terminal helix solvent exposed together with adjacent secondary elements forms an evolutionarily surface strong negative electrostatic potential. Several conditional mutant alleles S. cerevisiae MOB1 target this decrease net charge. Interestingly, kinases which yeast interact have two basic regions within their lobe. Thus, may regulate through interactions mediated charged surfaces.