8r3f

C-terminal Rel-homology Domain of NFAT1

spinqualitylabelsall models 8r3f, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8r3f is a 2 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 1.55Å Ligands: XS8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Transcription factors are generally considered challenging, if not "undruggable", targets but they promise new therapeutic options due to their fundamental involvement in many diseases. In this study, we aim to assess the ligandability of the C-terminal Rel-homology domain of nuclear factor of activated T cells 1 (NFAT1), a TF implicated in T-cell regulation. Using a combination of experimental and computational approaches, we demonstrate that small molecule fragments can indeed bind to this protein domain. The newly identified binder is the first small molecule binder to NFAT1 validated with biophysical methods and an elucidated binding mode by X-ray crystallography. The reported eutomer/distomer pair provides a strong basis for potential exploration of higher potency binders on the path toward degrader or glue modalities. Ligandability assessment of the C-terminal Rel-homology domain of NFAT1.,Bottcher J, Fuchs JE, Mayer M, Kahmann J, Zak KM, Wunberg T, Woehrle S, Kessler D Arch Pharm (Weinheim). 2024 Jun;357(6):e2300649. doi: 10.1002/ardp.202300649. , Epub 2024 Feb 23. PMID:38396281 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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