3cph: Difference between revisions

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[[Image:3cph.~~jpg~~|left|200px]]

[[Image:3cph.png|left|200px]]

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~~'''~~Crystal structure of Sec4 in complex with Rab-GDI~~'''~~

===Crystal structure of Sec4 in complex with Rab-GDI===

~~==Overview==~~

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~~RabGDI-facilitated extraction of prenylated Rab proteins from membranes plays an important role in vesicular membrane trafficking.~~ The ~~investigated thermodynamic properties of yeast Rab:GDI and Rab:MRS6 complexes demonstrated differences in the Rab binding properties of the closely related RabGDI and MRS6 proteins~~, consistent with their functional diversity. The importance of the Rab C-terminus and its prenylation for GDI/MRS6 binding was demonstrated using both biochemical and structural data. The presented structures of the apo-form yeast RabGDI and its two complexes with unprenylated Rab proteins, ~~together with~~ the ~~earlier published structures of~~ the ~~prenylated Ypt1~~:~~RabGDI provide evidence of allosteric regulation of the GDI lipid binding site opening~~, ~~which plays a key role in~~ the proposed mechanism of GDI mediated Rab extraction. We suggest a model for the interaction of GDI with prenylated Rab proteins which incorporates a stepwise increase in affinity as the 3 different partial interactions are successively formed.

The line below this paragraph, {{ABSTRACT_PUBMED_18426803}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18426803 is the PubMed ID number.

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==About this Structure==

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[[Category: Rab gtpase]]

[[Category: Vesicular transport]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~May 7~~ 08:56:42 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:56:09 2008''

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-[[Image:3cph.jpg|left|200px]]
+{{Seed}}
+[[Image:3cph.png|left|200px]]
 <!--
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 {{STRUCTURE_3cph|  PDB=3cph  |  SCENE=  }}
-'''Crystal structure of Sec4 in complex with Rab-GDI'''
+===Crystal structure of Sec4 in complex with Rab-GDI===
-==Overview==
+<!--
-RabGDI-facilitated extraction of prenylated Rab proteins from membranes plays an important role in vesicular membrane trafficking. The investigated thermodynamic properties of yeast Rab:GDI and Rab:MRS6 complexes demonstrated differences in the Rab binding properties of the closely related RabGDI and MRS6 proteins, consistent with their functional diversity. The importance of the Rab C-terminus and its prenylation for GDI/MRS6 binding was demonstrated using both biochemical and structural data. The presented structures of the apo-form yeast RabGDI and its two complexes with unprenylated Rab proteins, together with the earlier published structures of the prenylated Ypt1:RabGDI provide evidence of allosteric regulation of the GDI lipid binding site opening, which plays a key role in the proposed mechanism of GDI mediated Rab extraction. We suggest a model for the interaction of GDI with prenylated Rab proteins which incorporates a stepwise increase in affinity as the 3 different partial interactions are successively formed.
+The line below this paragraph, {{ABSTRACT_PUBMED_18426803}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18426803 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18426803}}
 ==About this Structure==
@@ Line 41: / Line 45: @@
 [[Category: Rab gtpase]]
 [[Category: Vesicular transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  7 08:56:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:56:09 2008''