The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue
M Hirshberg, RW Stockley, G Dodson… - Nature structural …, 1997 - nature.com
M Hirshberg, RW Stockley, G Dodson, MR Webb
Nature structural biology, 1997•nature.comThe crystal structure of human racl, a member of the rho family of small G-proteins,
complexed with the non-hydrolysable GTP analogue, guanosine-5′-(βγ-imino)
triphosphate (GMPPNP), has been determined by X-ray analysis at a resolution of 1.38 Å.
Comparison with the structure of H-ras indicates that racl has an extra α-helical domain that
is characteristic of the rho G proteins, and may be involved in the signalling pathway of this
family.
complexed with the non-hydrolysable GTP analogue, guanosine-5′-(βγ-imino)
triphosphate (GMPPNP), has been determined by X-ray analysis at a resolution of 1.38 Å.
Comparison with the structure of H-ras indicates that racl has an extra α-helical domain that
is characteristic of the rho G proteins, and may be involved in the signalling pathway of this
family.
Abstract
The crystal structure of human racl, a member of the rho family of small G-proteins, complexed with the non-hydrolysable GTP analogue, guanosine-5′-(βγ-imino)triphosphate (GMPPNP), has been determined by X-ray analysis at a resolution of 1.38 Å. Comparison with the structure of H-ras indicates that racl has an extra α-helical domain that is characteristic of the rho G proteins, and may be involved in the signalling pathway of this family.
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