Identification and analysis of protein phosphatases: A structural approach

초록

Protein phosphorylation and dephosphorylation are the well-characterized biochemical processes for reversible regulation of protein activities which are mediated by protein kinases and phosphatases. Recent studies suggest the presence of more than 500 protein kinases in mammals while the exact number of the complementary players remains obscure. Here we describe the catalog of human, mouse and rat protein phosphatases. Extensive in silico studies identified 179 human, 177 mouse and 176 rat protein phosphatases and 16 human, 18 mouse and 20 rat protein phosphatase pseudogenes. Human has orthologous for 171 mouse and rat protein phosphatases. Twenty one protein phosphatase families are existed in all three lineages. We have determined the 3D structure of catalytic domains of 17 family members using homology-based modeling systems. These catalytic domain structures were useful to construct a 3D structure space map of protein phosphatases. We showed that protein phosphatase catalytic domains are existed as three different folds.

제목
Identification and analysis of protein phosphatases: A structural approach
저자
SOH JAEWON
학회명
66th KSBMB meeting
개최지
COEX