The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms

Greasley, Samantha E., Jhoti, Harren, Teahan, Carmel, Solari, Roberto, Fensome, Amanda, Thomas, Geraint M H, Cockcroft, Shamshad and Bax, Ben ORCID: https://orcid.org/0000-0003-1940-3785 1995. The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms. Nature Structural and Molecular Biology 2 (9) , pp. 797-806. 10.1038/nsb0995-797

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Abstract

The ARFs are a family of 21,000 Mr proteins with biological roles in constitutive secretion and activation of phospholipase D. The structure of ARF-1 complexed to GDP determined from two crystal forms reveals a topology that is similar to that of the protein p21 ras with two differences: an additional amino-terminal helix and an extra β-strand. The Mg2+ ion in ARF-1 displays a five-coordination sphere; this feature is not seen in p21 ras, due to a shift in the relative position of the DXXG motif between the two proteins. The occurrence of a dimer in one crystal form suggests that ARF-1 may dimerize during its biological function. The dimer interface involves a region of the ARF-1 molecule that is analogous to the effector domain in p21 ras and may mediate interactions with its effectors

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences
Publisher:	Nature Publishing Group
ISSN:	1545-9993
Date of Acceptance:	20 July 1995
Last Modified:	23 Oct 2022 14:03
URI:	https://orca.cardiff.ac.uk/id/eprint/112647

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