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| | {{STRUCTURE_1kbf| PDB=1kbf | SCENE= }} | | {{STRUCTURE_1kbf| PDB=1kbf | SCENE= }} |
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| - | '''Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras'''
| + | ===Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras=== |
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| - | ==Overview==
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| - | Kinase suppressor of Ras (KSR) is a conserved component of the Ras pathway that acts as a molecular scaffold to promote signal transmission from Raf-1 to MEK and MAPK. All KSR proteins contain a conserved cysteine-rich C1 domain, and studies have implicated this domain in the regulation of KSR1 subcellular localization and function. To further elucidate the biological role of the KSR1 C1 domain, we have determined its three-dimensional solution structure using nuclear magnetic resonance (NMR). We find that while the overall topology of the KSR1 C1 domain is similar to the C1 domains of Raf-1 and PKCgamma, the predicted ligand-binding region and the surface charge distribution are unique. Moreover, by generating chimeric proteins in which these domains have been swapped, we find that the C1 domains of Raf-1, PKCgamma, and KSR1 are not functionally interchangeable. The KSR1 C1 domain does not bind with high affinity or respond biologically to phorbol esters or ceramide, and it does not interact directly with Ras, indicating that the putative ligand(s) for the KSR1 C1 domain are distinct from those that interact with PKCgamma and Raf-1. In addition, our analysis of the chimeric proteins supports the model that Raf-1 is a ceramide-activated kinase and that its C1 domain is involved in the ceramide-mediated response. Finally, our findings demonstrate an absolute requirement of the KSR1 C1 domain in mediating the membrane localization of KSR1, a crucial feature of its scaffolding activity. Together, these results underscore the functional specificity of these important regulatory domains and demonstrate that the structural features of the C1 domains can provide valuable insight into their ligand-binding properties.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11786023}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11786023 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11786023}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1KBF 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=1KBF OCA]. | + | 1KBF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBF OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Ksr]] | | [[Category: Ksr]] |
| | [[Category: Zinc-binding protein]] | | [[Category: Zinc-binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:32:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:04:53 2008'' |
Revision as of 07:04, 2 July 2008
Template:STRUCTURE 1kbf
Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras
Template:ABSTRACT PUBMED 11786023
About this Structure
1KBF is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.
Reference
Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR)., Zhou M, Horita DA, Waugh DS, Byrd RA, Morrison DK, J Mol Biol. 2002 Jan 18;315(3):435-46. PMID:11786023
Page seeded by OCA on Wed Jul 2 10:04:53 2008
