1lf5: Difference between revisions
New page: left|200px<br /> <applet load="1lf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lf5, resolution 1.70Å" /> '''Crystal Structure o... |
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'''Crystal Structure of RasA59G in the GDP-bound Form'''<br /> | '''Crystal Structure of RasA59G in the GDP-bound Form'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1LF5 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:// | 1LF5 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=1LF5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ras]] | [[Category: ras]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:17:53 2008'' | ||
Revision as of 17:17, 15 February 2008
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Crystal Structure of RasA59G in the GDP-bound Form
OverviewOverview
The conformational changes in Ras that accompany the hydrolysis of GTP are, critical to its function as a molecular switch in signaling pathways., Understanding how GTP is hydrolyzed by revealing the sequence of, intermediary structures in the reaction is essential for understanding Ras, signaling. Until now, no structure of an intermediate in GTP hydrolysis, has been experimentally determined for Ras alone. We have solved the, crystal structure of the Ala-59 to Gly mutant of Ras, (RasA59G), bound to, guanosine 5'-imidotriphosphate or GDP to 1.7-A resolution. In the, guanosine 5'-imidotriphosphate-bound form, this mutant adopts a, conformation that is intermediate between the GTP- and GDP-bound forms of, wild-type Ras and that is similar to what has been predicted by molecular, dynamics simulation [Ma, J. P. & Karplus, M. (1997) Proc. Natl. Acad. Sci., USA 94, 11905-11910]. This conformation is stabilized by direct and, water-mediated interactions between the switch 1 and switch 2 regions and, is characterized by an increase in the binding affinity for GTP. We, propose that the structural changes promoted by the Ala-59 to Gly mutation, exhibit a discrete conformational state assumed by wild-type Ras during, GTP hydrolysis.
DiseaseDisease
Known diseases associated with this structure: Bladder cancer, somatic OMIM:[190020], Costello syndrome OMIM:[190020], Thyroid carcinoma, follicular, somatic OMIM:[190020]
About this StructureAbout this Structure
1LF5 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The structural basis for the transition from Ras-GTP to Ras-GDP., Hall BE, Bar-Sagi D, Nassar N, Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12138-42. Epub 2002 Sep 4. PMID:12213964
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