3rfj

Design of a binding scaffold based on variable lymphocyte receptors of jawless vertebrates by module engineering

spinqualitylabelsall models 3rfj, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rfj is a 1 chain structure with sequence from Lism2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 3rfs Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Repeat proteins have recently been of great interest as potential alternatives to immunoglobulin antibodies due to their unique structural and biophysical features. We here present the development of a binding scaffold based on variable lymphocyte receptors, which are nonimmunoglobulin antibodies composed of Leucine-rich repeat modules in jawless vertebrates, by module engineering. A template scaffold was first constructed by joining consensus repeat modules between the N- and C-capping motifs of variable lymphocyte receptors. The N-terminal domain of the template scaffold was redesigned based on the internalin-B cap by analyzing the modular similarity between the respective repeat units using a computational approach. The newly designed scaffold, termed "Repebody," showed a high level of soluble expression in bacteria, displaying high thermodynamic and pH stabilities. Ease of molecular engineering was shown by designing repebodies specific for myeloid differentiation protein-2 and hen egg lysozyme, respectively, by a rational approach. The crystal structures of designed repebodies were determined to elucidate the structural features and interaction interfaces. We demonstrate general applicability of the scaffold by selecting repebodies with different binding affinities for interleukin-6 using phage display. Design of a binding scaffold based on variable lymphocyte receptors of jawless vertebrates by module engineering.,Lee SC, Park K, Han J, Lee JJ, Kim HJ, Hong S, Heu W, Kim YJ, Ha JS, Lee SG, Cheong HK, Jeon YH, Kim D, Kim HS Proc Natl Acad Sci U S A. 2012 Feb 28;109(9):3299-304. Epub 2012 Feb 10. PMID:22328160 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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