2a26
From Proteopedia
(New page: 200px<br /> <applet load="2a26" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a26, resolution 1.20Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2a26.gif|left|200px]]<br /> | + | [[Image:2a26.gif|left|200px]]<br /><applet load="2a26" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2a26" size=" | + | |
caption="2a26, resolution 1.20Å" /> | caption="2a26, resolution 1.20Å" /> | ||
'''Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein'''<br /> | '''Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Siah1 is the central component of a multiprotein E3 ubiquitin ligase | + | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2A26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and CXS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2A26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CXS:'>CXS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A26 OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ely, K | + | [[Category: Ely, K R.]] |
[[Category: Fukushima, T.]] | [[Category: Fukushima, T.]] | ||
[[Category: Leone, M.]] | [[Category: Leone, M.]] | ||
[[Category: Li, C.]] | [[Category: Li, C.]] | ||
| - | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
[[Category: Matsuzawa, S.]] | [[Category: Matsuzawa, S.]] | ||
| - | [[Category: Olson, A | + | [[Category: Olson, A J.]] |
[[Category: Pellecchia, M.]] | [[Category: Pellecchia, M.]] | ||
| - | [[Category: Preece, N | + | [[Category: Preece, N E.]] |
| - | [[Category: Reed, J | + | [[Category: Reed, J C.]] |
[[Category: Santelli, E.]] | [[Category: Santelli, E.]] | ||
[[Category: CXS]] | [[Category: CXS]] | ||
| Line 33: | Line 32: | ||
[[Category: helical hairpin]] | [[Category: helical hairpin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:51 2008'' |
Revision as of 14:22, 21 February 2008
|
Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein
Contents |
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.
Disease
Known disease associated with this structure: Mowat-Wilson syndrome OMIM:[605802]
About this Structure
2A26 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex., Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S, J Biol Chem. 2005 Oct 7;280(40):34278-87. Epub 2005 Aug 4. PMID:16085652
Page seeded by OCA on Thu Feb 21 16:22:51 2008
Categories: Homo sapiens | Single protein | Ely, K R. | Fukushima, T. | Leone, M. | Li, C. | Liddington, R C. | Matsuzawa, S. | Olson, A J. | Pellecchia, M. | Preece, N E. | Reed, J C. | Santelli, E. | CXS | SO4 | Dimerization | Helical hairpin
