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PROTEIN TYROSINE PHOSPHATASE: DECIPHERING CATALYTIC MECH & SUBSTRATE SPECIFICITY

PROTEIN TYROSINE PHOSPHATASE: DECIPHERING CATALYTIC MECH & SUBSTRATE SPECIFICITY
蛋白质酪氨酸磷酸酶：破译催化机制
批准号：
6281304
负责人：
MARK A SAPER
金额：
$1.92万
依托单位：
CORNELL UNIVERSITY
依托单位国家：
美国
项目类别：
财政年份：
1998
资助国家：
美国
项目状态：
已结题
起止时间：
1998-09-15 至 1999-08-14
来源：
https://reporter.nih.gov/project-details/6281304
关键词：
biological products biomedical resource proteins radiography structural biology

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We collected an outstanding data set from a crystals of the dual specificity phosphatase VHR complexed with vanadate. The data extended to at least 1.6 , and had an Rsym of 3.5% to 1.8 . This structure recently has been solved and provides insights into the transition state of phosphate hydrolysis. Several data sets were also collected from the catalytic domain of the LAR receptor tyrosine phosphatase. Data collected from frozen crystals of an anti-DNA Fab fragment are now being used to refine the structure of this antibody.
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