Fig. 4: KNL1C forms multiple interactions with MIS12C. | Nature Structural & Molecular Biology

Fig. 4: KNL1C forms multiple interactions with MIS12C.

From: Structure of the human outer kinetochore KMN network complex

Fig. 4: KNL1C forms multiple interactions with MIS12C.The alternative text for this image may have been generated using AI.

a, Overview of the MIS12C–KNL1C interface. The pair of RWD domains of Knl1 dominate this interface. b, Molecular details of the Knl1RWD-C interaction with MIS12C stalk, formed by Trp2249 docking into shallow grooves of the MIS12C central stalk and additionally supported by a number of electrostatic interactions on the opposite end of the Knl1RWD-C. c, The Nsl1 C-terminal peptide augments the central Knl1RWD-C β-sheet interaction with MIS12C, forming additional contacts with Knl1RWD-N.

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