2ogb
From Proteopedia
(New page: 200px<br /><applet load="2ogb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ogb, resolution 1.950Å" /> '''Crystal structure o...) |
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| - | [[Image:2ogb.gif|left|200px]]<br /><applet load="2ogb" size=" | + | [[Image:2ogb.gif|left|200px]]<br /><applet load="2ogb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ogb, resolution 1.950Å" /> | caption="2ogb, resolution 1.950Å" /> | ||
'''Crystal structure of the C-terminal domain of mouse Nrdp1'''<br /> | '''Crystal structure of the C-terminal domain of mouse Nrdp1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The E3 ubiquitin ligase neuregulin receptor degrading protein 1 (Nrdp1) | + | The E3 ubiquitin ligase neuregulin receptor degrading protein 1 (Nrdp1) mediates the ligand-independent degradation of the epidermal growth factor receptor family member ErbB3/HER3. By regulating cellular levels of ErbB3, Nrdp1 influences ErbB3-mediated signaling, which is essential for normal vertebrate development. Nrdp1 belongs to the tripartite or RBCC (RING, B-box, coiled-coil) family of ubiquitin ligases in which the RING domain is responsible for ubiquitin ligation and a variable C-terminal region mediates substrate recognition. We report here the 1.95 A crystal structure of the C-terminal domain of Nrdp1 and show that this domain is sufficient to mediate ErbB3 binding. Furthermore, we have used site-directed mutagenesis to map regions of the Nrdp1 surface that are important for interacting with ErbB3 and mediating its degradation in transfected cells. The ErbB3-binding site localizes to a region of Nrdp1 that is conserved from invertebrates to vertebrates, in contrast to ErbB3, which is only found in vertebrates. This observation suggests that Nrdp1 uses a common binding site to recognize its targets in different species. |
==About this Structure== | ==About this Structure== | ||
| - | 2OGB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SCN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http:// | + | 2OGB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SCN:'>SCN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OGB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
[[Category: Bouyain, S.]] | [[Category: Bouyain, S.]] | ||
| - | [[Category: Leahy, D | + | [[Category: Leahy, D J.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: SCN]] | [[Category: SCN]] | ||
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[[Category: receptor-binding region]] | [[Category: receptor-binding region]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:18:09 2008'' |
Revision as of 16:18, 21 February 2008
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Crystal structure of the C-terminal domain of mouse Nrdp1
Overview
The E3 ubiquitin ligase neuregulin receptor degrading protein 1 (Nrdp1) mediates the ligand-independent degradation of the epidermal growth factor receptor family member ErbB3/HER3. By regulating cellular levels of ErbB3, Nrdp1 influences ErbB3-mediated signaling, which is essential for normal vertebrate development. Nrdp1 belongs to the tripartite or RBCC (RING, B-box, coiled-coil) family of ubiquitin ligases in which the RING domain is responsible for ubiquitin ligation and a variable C-terminal region mediates substrate recognition. We report here the 1.95 A crystal structure of the C-terminal domain of Nrdp1 and show that this domain is sufficient to mediate ErbB3 binding. Furthermore, we have used site-directed mutagenesis to map regions of the Nrdp1 surface that are important for interacting with ErbB3 and mediating its degradation in transfected cells. The ErbB3-binding site localizes to a region of Nrdp1 that is conserved from invertebrates to vertebrates, in contrast to ErbB3, which is only found in vertebrates. This observation suggests that Nrdp1 uses a common binding site to recognize its targets in different species.
About this Structure
2OGB is a Single protein structure of sequence from Mus musculus with and as ligands. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3., Bouyain S, Leahy DJ, Protein Sci. 2007 Apr;16(4):654-61. PMID:17384230
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