3kj4

Structure of rat Nogo receptor bound to 1D9 antagonist antibody

spinqualitylabelsall models 3kj4, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kj4 is a 6 chain structure with sequence from Mus musculus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: MAN, NAG, NDG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RTN4R_RAT Receptor for RTN4, OMG and MAG. Mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system. Acts in conjunction with RTN4 and LIGO1 in regulating neuronal precursor cell motility during cortical development (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Nogo-66 receptor (NgR1) is part of a signaling complex that inhibits axon regeneration in the CNS. Truncated soluble versions of NgR1 have been used successfully to promote axon regeneration in animal models of spinal cord injury, raising interest in this protein as a potential therapeutic target. The leucine-rich repeat (LRR) regions in NgR1 are flanked by N- and C-terminal disulfide-containing "cap" domains (LRRNT and LRRCT, respectively). In this work we show that, although functionally active, the NgR1(310)-Fc fusion protein contains mislinked and heterogeneous disulfide patterns in the LRRCT, and we report the generation of a series of variant molecules specifically designed to prevent this heterogeneity. Using these variants we explored the effects of modifying the NgR1 truncation site or the spacing between the NgR1 and Fc domains, or replacing cysteines within the NgR1 or IgG hinge regions. One variant, which incorporates subsititutions of Cys266 and Cys309 with alanines, completely eliminated disulfide scrambling, while maintaining functional in vitro and in vivo efficacy. This modified NgR1-Fc molecule represents a significantly improved candidate for further pharmaceutical development, and may serve as a useful model for the optimization of other IgG fusion proteins made from LRR proteins. Resolution of disulfide heterogeneity in Nogo receptor 1 fusion proteins by molecular engineering.,Weinreb PH, Wen D, Qian F, Wildes CP, Garber EA, Walus L, Jung MY, Wang J, Relton JK, Amatucci J, Wang R, Porreca F, Silvian L, Meier W, Pepinsky RB, Lee DH Biotechnol Appl Biochem. 2010 Sep 3. PMID:20815818 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monoclonal Antibodies 3D structures

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