CENP-B is an 80 kDa protein. There is a DNA-binding region at the N-terminus. The crystal structure of CENP-B1-129 can be divided into four well-defined regions: the N-terminal arm (amino acid residues 1-9), domain 1 (residues 10-64), the linker loop (residues 65-74) and domain 2 (residues 75-129). There is a helix-turn-helix motif at domains 1 and 2 of CENP-B1-129. It binds to adjacent major grooves of DNA. The CENP-B domains 1 and 2 themselves are similar to each other. Helix 3 of domain 1 lies along the major groove and recognizes the essential sequences in site 1. It bends the DNA grooves.
Reference: Tanaka, Y., Nureki, O., Kurumizaka, H., Fukai, S., Kawaguchi, S., Ikuta, M., Iwahara, J., Okazaki, T. and Yokoyama, S. (2001), Crystal structure of the CENP-B protein–DNA complex: the DNA-binding domains of CENP-B induce kinks in the CENP-B box DNA. The EMBO Journal, 20: 6612-6618. https://doi.org/10.1093/emboj/20.23.6612
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