2a25: Difference between revisions

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|PDB= 2a25 |SIZE=350|CAPTION= <scene name='initialview01'>2a25</scene>, resolution 2.20&Aring;
|PDB= 2a25 |SIZE=350|CAPTION= <scene name='initialview01'>2a25</scene>, resolution 2.20&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE= SIAH1, HUMSIAH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= SIAH1, HUMSIAH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|DOMAIN=
|RELATEDENTRY=[[1k2f|1K2F]], [[2a26|2A26]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a25 OCA], [http://www.ebi.ac.uk/pdbsum/2a25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a25 RCSB]</span>
}}
}}


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==Overview==
==Overview==
Siah1 is the central component of a multiprotein E3 ubiquitin ligase complex that targets beta-catenin for destruction in response to p53 activation. The E3 complex comprises, in addition to Siah1, Siah-interacting protein (SIP), the adaptor protein Skp1, and the F-box protein Ebi. Here we show that SIP engages Siah1 by means of two elements, both of which are required for mediating beta-catenin destruction in cells. An N-terminal dimerization domain of SIP sits across the saddle-shaped upper surface of Siah1, with two extended legs packing against the sides of Siah1 by means of a consensus PXAXVXP motif that is common to a family of Siah-binding proteins. The C-terminal domain of SIP, which binds to Skp1, protrudes from the lower surface of Siah1, and we propose that this surface provides the scaffold for bringing substrate and the E2 enzyme into apposition in the functional complex.
Siah1 is the central component of a multiprotein E3 ubiquitin ligase complex that targets beta-catenin for destruction in response to p53 activation. The E3 complex comprises, in addition to Siah1, Siah-interacting protein (SIP), the adaptor protein Skp1, and the F-box protein Ebi. Here we show that SIP engages Siah1 by means of two elements, both of which are required for mediating beta-catenin destruction in cells. An N-terminal dimerization domain of SIP sits across the saddle-shaped upper surface of Siah1, with two extended legs packing against the sides of Siah1 by means of a consensus PXAXVXP motif that is common to a family of Siah-binding proteins. The C-terminal domain of SIP, which binds to Skp1, protrudes from the lower surface of Siah1, and we propose that this surface provides the scaffold for bringing substrate and the E2 enzyme into apposition in the functional complex.
==Disease==
Known disease associated with this structure: Mowat-Wilson syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605802 605802]]


==About this Structure==
==About this Structure==
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[[Category: Reed, J C.]]
[[Category: Reed, J C.]]
[[Category: Santelli, E.]]
[[Category: Santelli, E.]]
[[Category: ZN]]
[[Category: protein-peptide complex]]
[[Category: protein-peptide complex]]


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