8f5q

Crystal structure of human PCNA in complex with the PIP box of FBH1

spinqualitylabelsall models 8f5q, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8f5q is a 6 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 1.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed F-box DNA helicase 1 (FBH1) is involved in the regulation of cell responses to replicative stress. FBH1 is recruited to stalled DNA replication fork by PCNA where it inhibits homologous recombination and catalyzes fork regression. Here, we report the structural basis for the molecular recognition of two distinctly different motifs of FBH1, FBH1(PIP) and FBH1(APIM), by PCNA. The crystal structure of PCNA in complex with FBH1(PIP) and analysis of NMR perturbations reveal overlapped FBH1(PIP) and FBH1(APIM) binding sites of PCNA and the dominant contribution of FBH1(PIP) in this interaction. Molecular insight into the PCNA-binding mode of FBH1.,Liu J, Chaves-Arquero B, Wei P, Tencer AH, Ruiz-Albor A, Zhang G, Blanco FJ, Kutateladze TG Structure. 2023 May 4;31(5):511-517.e3. doi: 10.1016/j.str.2023.03.004. Epub 2023 , Mar 28. PMID:36990095 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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