9nn4

BET BRD3-BD1 in complex with peptide 7.2

spinqualitylabelsall models 9nn4, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9nn4 is a 4 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.37Å Ligands: ACE, ALY, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease BRD3_HUMAN Note=A chromosomal aberration involving BRD3 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;9)(q14;q34) with NUT which produces a BRD3-NUT fusion protein. Function BRD3_HUMAN Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene. Publication Abstract from PubMed The large size of macrocyclic peptides discovered by mRNA display can hinder therapeutic development. Using size-restricted RaPID libraries and analysis of 40 published datasets, we show that potent binders are more reliably identified from libraries with at least nine randomised residues, providing guidance for mRNA display screen design. The effect of peptide size on target affinity in mRNA display-derived macrocyclic peptides.,Jing X, Suh J, Maxwell J, Patel K, Norman A, Reid XJ, Deshpande C, Low JKK, Payne RJ, Passioura T, Mackay JP Chem Commun (Camb). 2026 Jan 30. doi: 10.1039/d5cc06167a. PMID:41614404 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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