1rrf
From Proteopedia
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'''NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM''' | '''NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM''' | ||
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[[Category: Greasley, S E.]] | [[Category: Greasley, S E.]] | ||
[[Category: Jhoti, H.]] | [[Category: Jhoti, H.]] | ||
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| - | [[Category: | + | [[Category: Membrane trafficking]] |
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:49:26 2008'' | |
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Revision as of 04:49, 3 May 2008
NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM
Overview
The ARFs are a family of 21,000 M(r) 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 beta-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.
About this Structure
1RRF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms., Greasley SE, Jhoti H, Teahan C, Solari R, Fensome A, Thomas GM, Cockcroft S, Bax B, Nat Struct Biol. 1995 Sep;2(9):797-806. PMID:7552752 Page seeded by OCA on Sat May 3 07:49:26 2008
