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2ogb
From Proteopedia
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|PDB= 2ogb |SIZE=350|CAPTION= <scene name='initialview01'>2ogb</scene>, resolution 1.950Å | |PDB= 2ogb |SIZE=350|CAPTION= <scene name='initialview01'>2ogb</scene>, resolution 1.950Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= Rnf41 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Rnf41 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ogb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ogb OCA], [http://www.ebi.ac.uk/pdbsum/2ogb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ogb RCSB]</span> | ||
}} | }} | ||
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[[Category: Bouyain, S.]] | [[Category: Bouyain, S.]] | ||
[[Category: Leahy, D J.]] | [[Category: Leahy, D J.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SCN]] | ||
[[Category: e3 ubiquitin ligase]] | [[Category: e3 ubiquitin ligase]] | ||
[[Category: receptor-binding region]] | [[Category: receptor-binding region]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:17:28 2008'' |
Revision as of 01:17, 31 March 2008
| |||||||
| , resolution 1.950Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | Rnf41 (Mus musculus) | ||||||
| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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