STRUCTURE OF LOW MOLECULAR WEIGHT TYROSINE PHOSPHATASES

低分子量酪氨酸磷酸酶的结构

• 批准号: 7420564
• 负责人: Cynthia Vianne Stauffacher
• 金额: $ 0.28万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-04-20 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7420564
• 关键词: active sites; enzymes; family; identity; metastasis; molecular weight; prenylation; protein tyrosine phosphatase; proteins; solutions; tyrosine

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. PTPCaaX-1 (PRL-1) represents a novel class of phosphatase, which has been implicated in triggering metastasis of cancerous cells. Like all protein tyrosine phosphatases, these enzymes contain the conserved active site motif (CX5R). Unique to these phosphatases is a nuclear localization sequence and the C-terminal CaaX box motif required for farnesylation. Sequence comparisons show the PRL proteins to be most similar to cdc14 and PTEN, sharing approximately 25% identity with each. However, this similarity is limited to a region of approximately 70 residues surrounding the active site, suggesting that the PRL enzymes constitute a new family of phosphatase. To date no structural information is available for any member of the PRL family. The detailed information obtained from a high-resolution, solution-state structure could ultimately prove valuable in breaking the link between overexpression of these enzymes and metastasis.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子弹和调查员（PI）可能已经从其他NIH来源获得了主要资金，因此可以在其他清晰的条目中代表。列出的机构适用于该中心，这不一定是调查员的机构。 PTPCAAX-1（PRL-1）代表了一类新型的磷酸酶，这与触发癌细胞转移有关。像所有蛋白质酪氨酸磷酸酶一样，这些酶含有保守的活性位点基序（CX5R）。这些磷酸酶独有的是核定位序列和Farnesylation所需的C末端CAAX盒基序。序列比较表明，PRL蛋白与CDC14和PTEN最相似，每个PET蛋白与每个人的身份共享约25％。但是，这种相似性仅限于活性位点周围约70个残基的区域，这表明PRL酶构成了一个新的磷酸酶家族。迄今为止，PRL家族的任何成员尚无结构信息。从高分辨率，溶液状态结构获得的详细信息最终可能证明在打破这些酶和转移之间的过表达之间的联系很有价值。