Article
Why does mutation of Gln61 in Ras by the nitro analog NGln maintain activity of Ras-GAP in hydrolysis of guanosine triphosphate?
Proteins - 1 Nov 2015
Khrenova Maria G, Grigorenko Bella L, Mironov Vladimir A, Nemukhin Alexander V
Abstract excerpt
Interpretation of the experiments showing that the Ras-GAP protein complex maintains activity in guanosine triphosphate (GTP) hydrolysis upon replacement of Glu61 in Ras with its unnatural nitro analog, NGln, is an important issue for understanding details of chemical transformations at the enzyme active site. By using molecular modeling we demonstrate that both glutamine and its nitro analog in the aci-nitro...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
