2ogb
From Proteopedia
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[[Image:2ogb.gif|left|200px]] | [[Image:2ogb.gif|left|200px]] | ||
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'''Crystal structure of the C-terminal domain of mouse Nrdp1''' | '''Crystal structure of the C-terminal domain of mouse Nrdp1''' | ||
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[[Category: Bouyain, S.]] | [[Category: Bouyain, S.]] | ||
[[Category: Leahy, D J.]] | [[Category: Leahy, D J.]] | ||
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Revision as of 07:51, 4 May 2008
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 Page seeded by OCA on Sun May 4 10:51:05 2008