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1bw6
From Proteopedia
(New page: 200px<br /> <applet load="1bw6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bw6" /> '''HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BIN...) |
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| - | [[Image:1bw6.gif|left|200px]]<br /> | + | [[Image:1bw6.gif|left|200px]]<br /><applet load="1bw6" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bw6" size=" | + | |
caption="1bw6" /> | caption="1bw6" /> | ||
'''HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BINDIGN DOMAIN RP1'''<br /> | '''HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BINDIGN DOMAIN RP1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CENP-B has been suggested to organize arrays of centromere satellite DNA | + | 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== | ==About this Structure== | ||
| - | 1BW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1BW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BW6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Masumoto, H.]] | [[Category: Masumoto, H.]] | ||
[[Category: Okazaki, T.]] | [[Category: Okazaki, T.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: centromere protein]] | [[Category: centromere protein]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:44 2008'' |
Revision as of 09:59, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 11:59:44 2008
Categories: Homo sapiens | Single protein | Iwahara, J. | Kigawa, T. | Kitagawa, K. | Masumoto, H. | Okazaki, T. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | Centromere protein | Dna-binding | Helix-turn-helix | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
