1s8f: Difference between revisions

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[[Image:1s8f.gif|left|200px]]
{{Seed}}
[[Image:1s8f.png|left|200px]]


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{{STRUCTURE_1s8f|  PDB=1s8f  |  SCENE=  }}  
{{STRUCTURE_1s8f|  PDB=1s8f  |  SCENE=  }}  


'''Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II'''
===Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II===




==Overview==
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The small GTPase Rab9 is an essential regulator of vesicular transport from the late endosome to the trans-Golgi network, as monitored by the redirection of the mannose-6-phosphate receptors. The crystal structure of Rab9 complexed to GDP, Mg(2+), and Sr(2+) reveals a unique dimer formed by an intermolecular beta-sheet that buries the switch I regions. Surface area and shape complementarity calculations suggest that Rab9 dimers can form an inactive, membrane-bound pool of Rab9 . GDP that is independent of GDI. Mg(2+)-bound Rab9 represents an inactive state, but Sr(2+)-bound Rab9 . GDP displays activated switch region conformations, mimicking those of the GTP state. A hydrophobic tetrad is formed resembling an effector-discriminating epitope found only in GTP-bound Rab proteins.
The line below this paragraph, {{ABSTRACT_PUBMED_15196914}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15196914}}


==About this Structure==
==About this Structure==
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[[Category: Intracellular transport]]
[[Category: Intracellular transport]]
[[Category: Vesicular trafficking]]
[[Category: Vesicular trafficking]]
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