PMC:4458296 / 6237-6945 JSONTXT

{"project":"2_test","denotations":[{"id":"26089585-20380929-25810851","span":{"begin":126,"end":127},"obj":"20380929"},{"id":"26089585-23509005-25810852","span":{"begin":129,"end":130},"obj":"23509005"},{"id":"26089585-22246954-25810853","span":{"begin":132,"end":134},"obj":"22246954"},{"id":"26089585-20380929-25810854","span":{"begin":489,"end":490},"obj":"20380929"},{"id":"26089585-23509005-25810855","span":{"begin":492,"end":493},"obj":"23509005"},{"id":"26089585-22246954-25810856","span":{"begin":495,"end":497},"obj":"22246954"}],"text":"2. PRPS1 Structure\nThe enzymatic active unit is a hexamer, consisting of three homodimers arranged in a propeller-like shape [1, 2, 17, 24]. Each of the homodimers has an active site and two regulatory allosteric sites, I and II. The active site allows for ATP and R5P to bind at the junction of two domains within one homodimer. Allosteric site I is located at the interface of the three homodimers and allosteric site II is located at the interface of two monomers within one homodimer [1, 2, 17, 24]. Mutations in the PRPS1 can either result in a gain of function with increased expression, PRPS1 superactivity, or result in a loss of function with a decreased expression, DFN-2, CMTX5, and Arts syndrome."}