1p2s: Difference between revisions

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[[Image:1p2s.~~jpg~~|left|200px]]

[[Image:1p2s.png|left|200px]]

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~~'''~~H-Ras 166 in 50% 2,2,2 triflouroethanol~~'''~~

===H-Ras 166 in 50% 2,2,2 triflouroethanol===

~~==Overview==~~

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~~Room temperature crystal structures of crosslinked H~~-~~Ras bound to GMPPNP were solved in 50% 2,2,2~~-~~trifluoroethanol, 60% 1,6-hexanediol, and 50% isopropanol.~~ The ~~disordered switch II region of Ras is ordered in the presence of 2~~,2,~~2-trifluoroethanol or 1,6-hexanediol. The overall backbone conformation of switch II in these organic solvents is~~ the ~~same as in~~ the ~~Ras-GMPPNP complexes with RalGDS, PI~~(3) ~~kinase~~, ~~and RasGAP, indicating a biologically relevant form. Key polar interactions that stabilize the ordered switch are enhanced in~~ the ~~presence of hydrophobic cosolvents~~. ~~These results suggest that hydrophobic solvents can be used in general to order short biologically relevant segments of disordered regions in protein crystals by favoring H~~-~~bonding interactions between atoms that are highly solvated and mobile in aqueous solution.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12842038}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12842038 is the PubMed ID number.

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==About this Structure==

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[[Category: Molecular switch protein]]

[[Category: Signaling protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 04~~:36:39 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:59:08 2008''

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-[[Image:1p2s.jpg|left|200px]]
+{{Seed}}
+[[Image:1p2s.png|left|200px]]
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 {{STRUCTURE_1p2s|  PDB=1p2s  |  SCENE=  }}
-'''H-Ras 166 in 50% 2,2,2 triflouroethanol'''
+===H-Ras 166 in 50% 2,2,2 triflouroethanol===
-==Overview==
+<!--
-Room temperature crystal structures of crosslinked H-Ras bound to GMPPNP were solved in 50% 2,2,2-trifluoroethanol, 60% 1,6-hexanediol, and 50% isopropanol. The disordered switch II region of Ras is ordered in the presence of 2,2,2-trifluoroethanol or 1,6-hexanediol. The overall backbone conformation of switch II in these organic solvents is the same as in the Ras-GMPPNP complexes with RalGDS, PI(3) kinase, and RasGAP, indicating a biologically relevant form. Key polar interactions that stabilize the ordered switch are enhanced in the presence of hydrophobic cosolvents. These results suggest that hydrophobic solvents can be used in general to order short biologically relevant segments of disordered regions in protein crystals by favoring H-bonding interactions between atoms that are highly solvated and mobile in aqueous solution.
+The line below this paragraph, {{ABSTRACT_PUBMED_12842038}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12842038 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12842038}}
 ==About this Structure==
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 [[Category: Molecular switch protein]]
 [[Category: Signaling protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:36:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:59:08 2008''