1hur
From Proteopedia
(New page: 200px<br /> <applet load="1hur" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hur, resolution 2.0Å" /> '''HUMAN ADP-RIBOSYLATI...) |
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| - | [[Image:1hur. | + | [[Image:1hur.jpg|left|200px]]<br /><applet load="1hur" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1hur, resolution 2.0Å" /> | caption="1hur, resolution 2.0Å" /> | ||
'''HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED'''<br /> | '''HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HUR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HUR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1HUR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: non-myristoylated]] | [[Category: non-myristoylated]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:58:18 2008'' |
Revision as of 13:58, 15 February 2008
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HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED
Overview
ADP-ribosylation factors (ARFs) are essential and ubiquitous in, eukaryotes, being involved in vesicular transport and functioning as an, activator of phospholipase D (refs 1, 2) and cholera toxin. The functions, of ARF proteins in membrane traffic and organelle integrity are intimately, tied to its reversible association with membranes and specific, interactions with membrane phospholipids. One common feature of these, functions is their regulation by the binding and hydrolysis of GTP. Here, we report the three-dimensional structure of full-length human ARF1 (M(r), 21,000) in its GDP-bound non-myristoylated form. The presence of a unique, amino-terminal alpha-helix and loop, together with differences in Mg2+, ligation and the existence of a non-crystallographic dimer, set this, structure apart from other GTP-binding proteins. These features provide a, structural basis for the GTP-dependent modulation of membrane affinity, the lack of intrinsic GTPase activity, and the nature of effector binding, surfaces.
About this Structure
1HUR is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the human ADP-ribosylation factor 1 complexed with GDP., Amor JC, Harrison DH, Kahn RA, Ringe D, Nature. 1994 Dec 15;372(6507):704-8. PMID:7990966
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