6sqc

Crystal structure of complex between nuclear coactivator binding domain of CBP and [1040-1086]ACTR containing alpha-methylated Leu1055 and Leu1076

spinqualitylabelsall models 6sqc, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6sqc is a 2 chain structure with sequence from Escherichia coli K-12 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.28Å Ligands: 2ML, EDO, GLC, PRD_900001, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Intrinsically disordered proteins (IDPs) constitute a large portion of "Dark Proteome" - difficult to characterize or yet to be discovered protein structures. Here we used conformationally constrained alpha-methylated amino acids to bias the conformational ensemble in the free unstructured activation domain of transcriptional coactivator ACTR. Different sites and patterns of substitutions were enabled by chemical protein synthesis and led to distinct populations of alpha-helices. A specific substitution pattern resulted in a substantially higher binding affinity to nuclear coactivator binding domain (NCBD) of CREB-binding protein, a natural binding partner of ACTR. The first X-ray structure of the modified ACTR domain - NCBD complex visualized a unique conformation of ACTR and confirmed that the key alpha-methylated amino acids are localized within alpha-helices in the bound state. This study demonstrates a strategy for characterization of individual conformational states of IDPs. Conformational editing of intrinsically disordered protein by alpha-methylation.,Bauer V, Schmidtgall B, Gogl G, Dolenc J, Osz J, Nomine Y, Kostmann C, Cousido-Siah A, Mitschler A, Rochel N, Trave G, Kieffer B, Torbeev V Chem Sci. 2020 Nov 4;12(3):1080-1089. doi: 10.1039/d0sc04482b. PMID:34163874 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Maltose-binding protein 3D structures Nuclear receptor coactivator

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