2ogb
From Proteopedia
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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 SCN and GOL 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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