8ir4

Crystal structure of the SLF1 BRCT domain in complex with a Rad18 peptide containing pS442

spinqualitylabelsall models 8ir4, resolution 1.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ir4 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.62Å Ligands: CL, IPA, MG, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Rad18 interacts with the SMC5/6 localization factor 1 (SLF1) to recruit the SMC5/6 complex to DNA damage sites for repair. The mechanism of the specific Rad18 recognition by SLF1 is unclear. Here, we present the crystal structure of the tandem BRCT repeat (tBRCT) in SLF1 (SLF1(tBRCT)) bound with the interacting Rad18 peptide. Our structure and biochemical studies demonstrate that SLF1(tBRCT) interacts with two phosphoserines and adjacent residues in Rad18 for high-affinity and specificity Rad18 recognition. We found that SLF1(tBRCT) utilizes mechanisms common among tBRCTs as well as unique ones for Rad18 binding, the latter include interactions with an alpha-helical structure in Rad18 that has not been observed in other tBRCT-bound ligand proteins. Our work provides structural insights into Rad18 targeting by SLF1 and expands the understanding of BRCT-mediated complex assembly. Structural insights into Rad18 targeting by the SLF1 BRCT domains.,Huang W, Qiu F, Zheng L, Shi M, Shen M, Zhao X, Xiang S J Biol Chem. 2023 Nov;299(11):105288. doi: 10.1016/j.jbc.2023.105288. Epub 2023 , Sep 23. PMID:37748650 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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