2lr2 | pdb_00002lr2

Designed IgG and lanthanide binding probe for solution NMR, MRI and luminescence microscopy

spinqualitylabelsall models 2lr2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lr2 is a 1 chain structure with sequence from Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Paramagnetic lanthanide ions when bound to proteins offer great potential for structural investigations that utilize solution nuclear magnetic resonance spectroscopy, magnetic resonance imaging, or optical microscopy. However, many proteins do not have native metal ion binding sites and engineering a chimeric protein to bind an ion while retaining affinity for a protein of interest represents a significant challenge. Here we report the characterization of an immunoglobulin G-binding protein redesigned to include a lanthanide binding motif in place of a loop between two helices (Z-L2LBT). It was shown to bind Tb(3+) with 130 nM affinity. Ions such as Dy(3+) , Yb(3+) , and Ce(3+) produce paramagnetic effects on NMR spectra and the utility of these effects is illustrated by their use in determining a structural model of the metal-complexed Z-L2LBT protein and a preliminary characterization of the dynamic distribution of IgG Fc glycan positions. Furthermore, this designed protein is demonstrated to be a novel IgG-binding reagent for magnetic resonance imaging (Z-L2LBT:Gd(3+) complex) and luminescence microscopy (Z-L2LBT: Tb(3+) complex). Lanthanide binding and IgG affinity construct: Potential applications in solution NMR, MRI, and luminescence microscopy.,Barb AW, Ho TG, Flanagan-Steet H, Prestegard JH Protein Sci. 2012 Jul 31. doi: 10.1002/pro.2133. PMID:22851279 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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