Large interface area normally means batter affinity (lower Kd).
CHL4-IML3 complex forms a U-shape groove which plays a vital role in initiating the interactions between the unwrapped DNA duplex and Cenp-A nucleosome ( located in centromere which helps assemble complete kinetochore) and therefore, it contributes significantly to chromosomes segregations. Additionally, CHL4 is important in coordinating CCAN subunits as it located in the centre of this protein [1].
MCM21 and CTF19 were found to be a part of a heterogeneous complex that distally located from Cenp-A nucleosome and serves as a repairing machine for spindle microtubules damage [2].
Among the residues involved in forming the CHL4-IML3 interface, on average, more than 50% of the residues within the binding groove are hydrophobic, which may be one of the reasons for the higher affinity between the two chains besides the complementary interfaces. Similar situations have also been found in the interface between CHL4-MCM21 and the interface of CHL4-CTF19.
CHL4-IML3 groove binding shape increases its affinity.
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Shape complementarity of CHL4-MCM21 also gives higher affinity.
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CHL4-CTF19 interface is also a groove shape.
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1. Yan, K., Jing, Y., Ziguo, Z., Stephen, M., Leifu, C., Domenico, F., Ann, E., Albert, J., and David, B., Structure of the inner kinetochore CCAN complex assembled onto a centromeric nucleosome. Nature, 2019. 574(7777): p. 278-282.
2. Perpelescu, M. and Fukagawa, T., The abcs of cenps. Chromosoma, 2011. 120(5): p. 425.
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