STRUCTURE OF THE SIGMA ISOFORM OF THE PHOSPHOPEPTIDE-BINDING PROTEIN 14-3-3

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 哺乳动物14-3-3蛋白家族的七种亚型在细胞内信号传导中发挥不同的作用。大多数14-3-3蛋白在不同同种型之间形成同源二聚体和混合异源二聚体，在配体结合中具有重叠作用。一种哺乳动物同种型，14-3-3 σ，似乎在细胞对DNA损伤的反应和人类肿瘤发生中发挥独特的作用。这些14-3-3 sigma特异性功能的生物学和结构基础尚不清楚。为了了解14-3-3 sigma优先同源二聚化的基础，并阐明其独特的功能特异性的机制，我们对sigma亚型进行了生化和结构研究。 关于这项工作的论文发表在J. Biol. Chem.

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The seven mammalian isoforms of 14-3-3 family of proteins play diverse roles in intracellular signaling. Most 14-3-3 proteins form homodimers and mixed heterodimers between different isotypes, with overlapping roles in ligand binding. One mammalian isoform, 14-3-3 sigma, appears to play a unique role in the cellular response to DNA damage and in human oncogenesis. The biological and structural basis for these 14-3-3 sigma-specific functions is unknown. To understand the basis for preferential homodimerization of 14-3-3 sigma and to shed light on mechanisms of its unique functional specificity we have conducted biochemical and structural studies on the sigma isoform. The paper on this work was published in J. Biol. Chem.