1lfd
From Proteopedia
(New page: 200px<br /> <applet load="1lfd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lfd, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1lfd.gif|left|200px]]<br /> | + | [[Image:1lfd.gif|left|200px]]<br /><applet load="1lfd" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lfd" size=" | + | |
caption="1lfd, resolution 2.1Å" /> | caption="1lfd, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS'''<br /> | '''CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Ras protein signals to a number of distinct pathways by interacting | + | The Ras protein signals to a number of distinct pathways by interacting with diverse downstream effectors. Among the effectors of Ras are the Raf kinase and RalGDS, a guanine nucleotide dissociation stimulator specific for Ral. Despite the absence of significant sequence similarities, both effectors bind directly to Ras, but with different specificities. We report here the 2.1 A crystal structure of the complex between Ras and the Ras-interacting domain (RID) of RalGDS. This structure reveals that the beta-sheet of the RID joins the switch I region of Ras to form an extended beta-sheet with a topology similar to that found in the Rap-Raf complex. However, the side chain interactions at the joining junctions of the two interacting systems and the relative orientation of the two binding domains are distinctly different. Furthermore, in the case of the Ras-RID complex a second RID molecule also interacts with a different part of the Ras molecule, the switch II region. These findings account for the cross-talk between the Ras and Ral pathways and the specificity with which Ras distinguishes the two effectors. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LFD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LFD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hofer, F.]] | [[Category: Hofer, F.]] | ||
[[Category: Huang, L.]] | [[Category: Huang, L.]] | ||
| - | [[Category: Kim, S | + | [[Category: Kim, S H.]] |
| - | [[Category: Martin, G | + | [[Category: Martin, G S.]] |
[[Category: GNP]] | [[Category: GNP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: ral]] | [[Category: ral]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:29 2008'' |
Revision as of 11:44, 21 February 2008
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CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS
Contents |
Overview
The Ras protein signals to a number of distinct pathways by interacting with diverse downstream effectors. Among the effectors of Ras are the Raf kinase and RalGDS, a guanine nucleotide dissociation stimulator specific for Ral. Despite the absence of significant sequence similarities, both effectors bind directly to Ras, but with different specificities. We report here the 2.1 A crystal structure of the complex between Ras and the Ras-interacting domain (RID) of RalGDS. This structure reveals that the beta-sheet of the RID joins the switch I region of Ras to form an extended beta-sheet with a topology similar to that found in the Rap-Raf complex. However, the side chain interactions at the joining junctions of the two interacting systems and the relative orientation of the two binding domains are distinctly different. Furthermore, in the case of the Ras-RID complex a second RID molecule also interacts with a different part of the Ras molecule, the switch II region. These findings account for the cross-talk between the Ras and Ral pathways and the specificity with which Ras distinguishes the two effectors.
Disease
Known diseases associated with this structure: Bladder cancer, somatic OMIM:[190020], Costello syndrome OMIM:[190020], Thyroid carcinoma, follicular, somatic OMIM:[190020]
About this Structure
1LFD is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for the interaction of Ras with RalGDS., Huang L, Hofer F, Martin GS, Kim SH, Nat Struct Biol. 1998 Jun;5(6):422-6. PMID:9628477
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