Greasley, Samantha E., Jhoti, Harren, Teahan, Carmel, Solari, Roberto, Fensome, Amanda, Thomas, Geraint M H, Cockcroft, Shamshad and Bax, Ben ![]() |
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 |
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Date Type: | Publication |
Status: | Published |
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 |
Citation Data
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