1rlf: Difference between revisions
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[[Image:1rlf.jpg|left|200px]] | [[Image:1rlf.jpg|left|200px]] | ||
'''STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES''' | {{Structure | ||
|PDB= 1rlf |SIZE=350|CAPTION= <scene name='initialview01'>1rlf</scene> | |||
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'''STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RLF is a [ | 1RLF is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9753431 9753431] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:13 2008'' | ||
Revision as of 11:53, 20 March 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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