1ysm
From Proteopedia
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| - | [[Image:1ysm.gif|left|200px]] | + | [[Image:1ysm.gif|left|200px]] |
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| - | '''NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.''' | + | {{Structure |
| + | |PDB= 1ysm |SIZE=350|CAPTION= <scene name='initialview01'>1ysm</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Cacybp, Sip ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YSM is a [ | + | 1YSM 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=1YSM OCA]. |
==Reference== | ==Reference== | ||
| - | The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies., Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ, Biochemistry. 2005 Jul 12;44(27):9462-71. PMID:[http:// | + | The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies., Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ, Biochemistry. 2005 Jul 12;44(27):9462-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15996101 15996101] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| - | ''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 15:26:57 2008'' |
Revision as of 13:26, 20 March 2008
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| Gene: | Cacybp, Sip (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.
Overview
Siah-interacting protein (SIP) was identified as a novel adaptor that physically links the E3 ubiquitin ligase activity of Siah-1 with Skp1 and Ebi F-Box protein in the degradation of beta-catenin, a transcriptional activator of TCF/LEF genes. In this study, we have used solution NMR spectroscopy to characterize the domain structure of SIP, which includes a novel helical hairpin domain at the N-terminus flexibly linked to a CS domain and an unstructured carboxy terminal SGS domain. These studies have been complemented by mapping the sites of functionally important protein-protein interactions involving Siah-1 and Skp1 to individual domains of SIP. NMR-based chemical shift perturbation assays show that Siah-1 interacts with the flexible linker between SIP N and CS domains. This site for interaction in the linker does not perturb residues in the structured region at the N-terminus but does appear to restrict the rotational freedom of the SIP CS domain in the context of the full-length protein. In contrast, Skp1 engages the SIP CS domain exclusively through weak interactions that are not coupled to the other domains. The principal role of the modular structure of SIP appears to be in bringing these two proteins into physical proximity and orchestrating the orientation required for polyubiquitination of beta-catenin in the intact SCF-type complex.
About this Structure
1YSM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies., Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ, Biochemistry. 2005 Jul 12;44(27):9462-71. PMID:15996101
Page seeded by OCA on Thu Mar 20 15:26:57 2008
