Fig. 2: The cyclin D1 E-rich region is necessary for the recognition of H2BS14P in Microscale Thermophoresis (MST) analysis. | Oncogenesis

Fig. 2: The cyclin D1 E-rich region is necessary for the recognition of H2BS14P in Microscale Thermophoresis (MST) analysis.

From: A cyclin D1 intrinsically disordered ___domain accesses modified histone motifs to govern gene transcription

Fig. 2

A MST analysis with H2B (A, C) and H2BS14P (B, D), indicating Kd, or the lack of binding (Kd cannot be determined, n.d.). E Human cyclin D1 (CD1) (Alpha fold – AF-P24385-F1) is shown in electrostatic surface and H2B (PDB ID: 2RVQ) [102] is shown in the sticks (green or magenta). Cyclin D1 contains a large negatively charged cavity on its surface which is ideal for binding to the highly positively charged tail of H2B. It is worth noting that this pocket is formed by helices α2, α 6, and α9 and is away from the CDK4/6 interacting site of cyclin D1. F 180° rotation of the structure in (E). G Cartoon representation of cyclin D1-H2B structural model. Helices α2, α6, and α9 that form the H2B binding pocket of cyclin D1 are shown, as well as the pS14 and the glutamates that form the E-rich region. H Zoom in on the representation of the interaction between cyclin D1 and H2B same orientation as in (H). Cyclin D1 is shown in wheat color. The E-region which binds S14P is shown in blue. The phosphoserine S14P is shown in magenta on the green sticks of the histone peptide.

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