Crystal structure of a human Mob1 protein: toward understanding Mob-regulated cell cycle pathways.
Crystal structure of a human Mob1 protein: toward understanding Mob-regulated cell cycle pathways.
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DOI：
10.1016/s0969-2126(03)00182-5
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发表时间：
2003-09
期刊：
影响因子：
5.7
通讯作者：
E. Stavridi;Kimberly G. Harris;Y. Huyen;J. Bothos;Peter-Mark Verwoerd;S. Stayrook;N. Pavletich;P. Je
中科院分区：
文献类型：
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作者：
E. Stavridi;Kimberly G. Harris;Y. Huyen;J. Bothos;Peter-Mark Verwoerd;S. Stayrook;N. Pavletich;P. Je
The Mob protein family comprises a group of highly conserved eukaryotic proteins whose founding member functions in the mitotic exit network. At the molecular level, Mob proteins act as kinase-activating subunits. We cloned a human Mob1 family member, Mob1A, and determined its three-dimensional structure by X-ray crystallography. The core of Mob1A consists of a four-helix bundle that is stabilized by a bound zinc atom. The N-terminal helix of the bundle is solvent exposed and together with adjacent secondary structure elements forms an evolutionarily conserved surface with a strong negative electrostatic potential. Several conditional mutant alleles ofS. cerevisiae MOB1target this surface and decrease its net negative charge. Interestingly, the kinases with which yeast Mob proteins interact have two conserved basic regions within their N-terminal lobe. Thus, Mob proteins may regulate their target kinases through electrostatic interactions mediated by conserved charged surfaces.
