DIRAS: Distinct subgroup of the Ras family, member 1 (human)
PDB Code: 2GF0
Cells respond in many ways to environmental changes including altering gene expression, physically moving locations, changes to cell-cell interactions, differentiation and even altering their life spans. This is achieved through a signalling network that consists of several signalling pathways. The network receives multiple signals, interprets the signals, amplified and then transmits the signals. One of the best characterised signalling pathways involves the ras GTPase family. The importance of this family of small GTPases to human health was first recognised through the identification of the human H-Ras, N-Ras and K-Ras genes as being oncogenic.
DIRAS1 is the second member of the subfamily of DIRAS small GTPases to have its crystal structure determined. In contrast to the classical Ras GTPase, DIRAS1 acts as a tumor repressor. The family members are characterised by a number of alterations that would be expected to produce a constitutively active form. The most significant is the lack of a glutamine residue, the equivalent of which is highly conserved in catalytically active small GTPases and is known to be involved in the catalysis process. DIRAS family members are also likely to use a different signalling pathway from the standard Ras-Raf-1 kinase signalling pathway as a hydrophobic residue is present in place of an Asp in Ras which forms part of the Ras-Raf-1 binding site.
Even though the DIRAS1 family are expected to exist mostly in the GTP bound active state they can turnover GTP and do have an inactive conformation. Here we have captured the structure of DIRAS1 in the inactive GDP bound state.
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