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HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BINDIGN DOMAIN RP1

Overview

CENP-B has been suggested to organize arrays of centromere satellite DNA, into a higher order structure which then directs centromere formation and, kinetochore assembly in mammalian chromosomes. The N-terminal portion of, CENP-B is a 15 kDa DNA binding domain (DBD) consisting of two repeating, units, RP1 and RP2. The DBD specifically binds to the CENP-B box sequence, (17 bp) in centromere DNA. We determined the solution structure of human, CENP-B DBD RP1 by multi-dimensional 1H, 13C and 15N NMR methods. The, CENP-B DBD RP1 structure consists of four helices and has a, helix-turn-helix structure. The overall folding is similar to those of, some other eukaryotic DBDs, although significant sequence homology with, these proteins was not found. The DBD of yeast RAP1, a telomere binding, protein, is most similar to CENP-B DBD RP1. We studied the interaction, between CENP-B DBD RP1 and the CENP-B box by the use of NMR chemical shift, perturbation. The results suggest that CENP-B DBD RP1 interacts with one, of the essential regions of the CENP-B box DNA, mainly at the N-terminal, basic region, the N-terminal portion of helix 2 and helix 3.

About this Structure

1BW6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A helix-turn-helix structure unit in human centromere protein B (CENP-B)., Iwahara J, Kigawa T, Kitagawa K, Masumoto H, Okazaki T, Yokoyama S, EMBO J. 1998 Feb 2;17(3):827-37. PMID:9451007

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