1wq1
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1wq1.gif|left|200px]] | [[Image:1wq1.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1wq1", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1wq1| PDB=1wq1 | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''RAS-RASGAP COMPLEX''' | '''RAS-RASGAP COMPLEX''' | ||
| Line 32: | Line 29: | ||
[[Category: Wiesmueller, L.]] | [[Category: Wiesmueller, L.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
| - | [[Category: | + | [[Category: Gap]] |
| - | [[Category: | + | [[Category: Growth regulation]] |
| - | + | [[Category: Gtp hydrolysis]] | |
| - | [[Category: | + | [[Category: Ra]] |
| - | [[Category: | + | [[Category: Signal transduction]] |
| - | [[Category: | + | [[Category: Transition state]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:59:54 2008'' |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:59, 3 May 2008
RAS-RASGAP COMPLEX
Overview
The three-dimensional structure of the complex between human H-Ras bound to guanosine diphosphate and the guanosine triphosphatase (GTPase)-activating domain of the human GTPase-activating protein p120GAP (GAP-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. The structure shows the partly hydrophilic and partly hydrophobic nature of the communication between the two molecules, which explains the sensitivity of the interaction toward both salts and lipids. An arginine side chain (arginine-789) of GAP-334 is supplied into the active site of Ras to neutralize developing charges in the transition state. The switch II region of Ras is stabilized by GAP-334, thus allowing glutamine-61 of Ras, mutation of which activates the oncogenic potential, to participate in catalysis. The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations. Glycine-12 in the transition state mimic is within van der Waals distance of both arginine-789 of GAP-334 and glutamine-61 of Ras, and even its mutation to alanine would disturb the arrangements of residues in the transition state.
About this Structure
1WQ1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants., Scheffzek K, Ahmadian MR, Kabsch W, Wiesmuller L, Lautwein A, Schmitz F, Wittinghofer A, Science. 1997 Jul 18;277(5324):333-8. PMID:9219684 Page seeded by OCA on Sat May 3 13:59:54 2008
