Ontology highlight
ABSTRACT:
SUBMITTER: Knihtila R
PROVIDER: S-EPMC4692228 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20151029 52
RAS GTPase is a prototype for nucleotide-binding proteins that function by cycling between GTP and GDP, with hydrogen atoms playing an important role in the GTP hydrolysis mechanism. It is one of the most well studied proteins in the superfamily of small GTPases, which has representatives in a wide range of cellular functions. These proteins share a GTP-binding pocket with highly conserved motifs that promote hydrolysis to GDP. The neutron crystal structure of RAS presented here strongly support ...[more]