1rlf
From Proteopedia
(New page: 200px<br /><applet load="1rlf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rlf" /> '''STRUCTURE DETERMINATION OF THE RAS-BINDING D...) |
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| - | [[Image:1rlf.jpg|left|200px]]<br /><applet load="1rlf" size=" | + | [[Image:1rlf.jpg|left|200px]]<br /><applet load="1rlf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rlf" /> | caption="1rlf" /> | ||
'''STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES'''<br /> | '''STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ral-specific guanine nucleotide exchange factors RalGDS, Rgl, and Rlf have | + | Ral-specific guanine nucleotide exchange factors RalGDS, Rgl, and Rlf have been suggested to function as intermediates between Ras and Ral pathways by being able to bind Ras proteins through their C-terminal Ras-binding domains (RBD). The RBDs of RalGDS and of the Ser/Thr kinase c-Raf-1 have been shown to have the same tertiary structure. In contrast to the RBDs of Raf and RalGDS, which bind either Ras or Rap with high affinity, Rlf-RBD has a similar affinity for both GTP-binding proteins. To be able to compare these RBDs on a structural level, we have solved the three-dimensional structure of Rlf-RBD by NMR spectroscopy. The overall tertiary structure of Rlf-RBD shows the betabetaalphabetabetaalphabeta-fold of the ubiquitin superfamily and is very similar to that of RalGDS-RBD. The binding interface of Rlf-RBD to Ras was mapped using chemical shift analysis and indicated a binding mode similar to that in the case of Rap.Raf-RBD. However, comparison of the putatively interacting regions revealed structural differences which are proposed to be responsible for the different substrate affinities of Rlf-, RalGDS-, and Raf-RBD. |
==About this Structure== | ==About this Structure== | ||
| - | 1RLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1RLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bauer, B.]] | [[Category: Bauer, B.]] | ||
[[Category: Bay, P.]] | [[Category: Bay, P.]] | ||
| - | [[Category: Cool, R | + | [[Category: Cool, R H.]] |
[[Category: Esser, D.]] | [[Category: Esser, D.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
| - | [[Category: Wolthuis, R | + | [[Category: Wolthuis, R M.F.]] |
[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:08 2008'' |
Revision as of 12:52, 21 February 2008
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STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES
Overview
Ral-specific guanine nucleotide exchange factors RalGDS, Rgl, and Rlf have been suggested to function as intermediates between Ras and Ral pathways by being able to bind Ras proteins through their C-terminal Ras-binding domains (RBD). The RBDs of RalGDS and of the Ser/Thr kinase c-Raf-1 have been shown to have the same tertiary structure. In contrast to the RBDs of Raf and RalGDS, which bind either Ras or Rap with high affinity, Rlf-RBD has a similar affinity for both GTP-binding proteins. To be able to compare these RBDs on a structural level, we have solved the three-dimensional structure of Rlf-RBD by NMR spectroscopy. The overall tertiary structure of Rlf-RBD shows the betabetaalphabetabetaalphabeta-fold of the ubiquitin superfamily and is very similar to that of RalGDS-RBD. The binding interface of Rlf-RBD to Ras was mapped using chemical shift analysis and indicated a binding mode similar to that in the case of Rap.Raf-RBD. However, comparison of the putatively interacting regions revealed structural differences which are proposed to be responsible for the different substrate affinities of Rlf-, RalGDS-, and Raf-RBD.
About this Structure
1RLF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf., Esser D, Bauer B, Wolthuis RM, Wittinghofer A, Cool RH, Bayer P, Biochemistry. 1998 Sep 29;37(39):13453-62. PMID:9753431
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