Title : Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation.

Pub. Date : 1999 Feb

PMID : 10048930






2 Functional Relationships(s)
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Protein Name
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1 Mutation of Asp 262, located 5.5 A distal to the active site, demonstrates it is essential for catalysis in the high-activity ERK2-dependent conformation of Pyst1 but not for the low-activity ERK2-independent form, suggesting that ERK2 induces closure of the Asp 262 loop over the active site, thereby enhancing Pyst1 catalytic efficiency. Aspartic Acid mitogen-activated protein kinase 1 Homo sapiens
2 Mutation of Asp 262, located 5.5 A distal to the active site, demonstrates it is essential for catalysis in the high-activity ERK2-dependent conformation of Pyst1 but not for the low-activity ERK2-independent form, suggesting that ERK2 induces closure of the Asp 262 loop over the active site, thereby enhancing Pyst1 catalytic efficiency. Aspartic Acid mitogen-activated protein kinase 1 Homo sapiens