5mfg

Designed armadillo repeat protein YIIIM5AII in complex with peptide (RR)4

spinqualitylabelsall models 5mfg, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mfg is a 5 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.901Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Designed armadillo repeat proteins (dArmRP) were developed to create a modular peptide binding technology where each of the structural repeats binds two residues of the target peptide. An essential prerequisite for such a technology is a dArmRP geometry that matches the peptide bond length. To this end, we determined a large set (n=27) of dArmRP X-ray structures, of which 14 were previously unpublished, to calculate curvature parameters that define their geometry. Our analysis shows that consensus dArmRPs exhibit curvatures close to the optimal range for modular peptide recognition. Binding of peptide ligands can induce a curvature within the desired range, as confirmed by single-molecule FRET experiments in solution. On the other hand, computationally designed ArmRPs, where side chains have been chosen with the intention to optimally fit into a geometrically optimized backbone, turned out to be more divergent in reality, and thus not suitable for continuous peptide binding. Furthermore, we show that the formation of a crystal lattice can induce small but significant deviations from the curvature adopted in solution, which can interfere with the evaluation of repeat protein scaffolds when high accuracy is required. This study corroborates the suitability of consensus dArmRP as a scaffold for the development of modular peptide binders. Curvature of designed armadillo repeat proteins allows modular peptide binding.,Hansen S, Ernst P, Konig SLB, Reichen C, Ewald C, Nettels D, Mittl PRE, Schuler B, Pluckthun A J Struct Biol. 2017 Aug 29. pii: S1047-8477(17)30140-5. doi:, 10.1016/j.jsb.2017.08.009. PMID:28864298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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