1rrg: Difference between revisions

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New page: left|200px<br /><applet load="1rrg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rrg, resolution 2.4Å" /> '''NON-MYRISTOYLATED RAT...
 
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[[Image:1rrg.jpg|left|200px]]<br /><applet load="1rrg" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rrg.jpg|left|200px]]<br /><applet load="1rrg" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rrg, resolution 2.4&Aring;" />
caption="1rrg, resolution 2.4&Aring;" />
'''NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM'''<br />
'''NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM'''<br />


==Overview==
==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.
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==
==About this Structure==
1RRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RRG OCA].  
1RRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRG OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bax, B.]]
[[Category: Bax, B.]]
[[Category: Greasley, S.E.]]
[[Category: Greasley, S E.]]
[[Category: Jhoti, H.]]
[[Category: Jhoti, H.]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: transport protein]]
[[Category: transport protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:49:17 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:47 2008''