1BW6

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

Summary for 1BW6

• Entry DOI: 10.2210/pdb1bw6/pdb
• Descriptor: PROTEIN (CENTROMERE PROTEIN B) (1 entity in total)
• Functional Keywords: centromere protein, dna-binding, helix-turn-helix, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P07199
• Total number of polymer chains: 1
• Total formula weight: 6546.63

Authors

Iwahara, J.,Kigawa, T.,Kitagawa, K.,Masumoto, H.,Okazaki, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1998-09-30, release date: 1998-10-07, Last modification date: 2024-05-22)

Primary citation

Iwahara, J.,Kigawa, T.,Kitagawa, K.,Masumoto, H.,Okazaki, T.,Yokoyama, S.
A helix-turn-helix structure unit in human centromere protein B (CENP-B).
EMBO J., 17:827-837, 1998

PubMed Abstract: 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.

PubMed: 9451007
DOI: 10.1093/emboj/17.3.827

Experimental method

SOLUTION NMR