1ufi
From Proteopedia
(New page: 200px<br /> <applet load="1ufi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ufi, resolution 1.65Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ufi.gif|left|200px]]<br /> | + | [[Image:1ufi.gif|left|200px]]<br /><applet load="1ufi" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ufi" size=" | + | |
caption="1ufi, resolution 1.65Å" /> | caption="1ufi, resolution 1.65Å" /> | ||
'''Crystal structure of the dimerization domain of human CENP-B'''<br /> | '''Crystal structure of the dimerization domain of human CENP-B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human centromere protein B (CENP-B), a centromeric heterochromatin | + | The human centromere protein B (CENP-B), a centromeric heterochromatin component, forms a homodimer that specifically binds to a distinct DNA sequence (the CENP-B box), which appears within every other alpha-satellite repeat. Previously, we determined the structure of the human CENP-B DNA-binding domain, CENP-B-(1-129), complexed with the CENP-B box DNA. In the present study, we determined the crystal structure of its dimerization domain (CENP-B-(540-599)), another functional domain of CENP-B, at 1.65-A resolution. CENP-B-(540-599) contains two alpha-helices, which are folded into an antiparallel configuration. The CENP-B-(540-599) dimer formed a symmetrical, antiparallel, four-helix bundle structure with a large hydrophobic patch in which 23 residues of one monomer form van der Waals contacts with the other monomer. In the CENP-B-(540-599) dimer, the N-terminal ends of CENP-B-(540-599) are oriented on opposite sides of the dimer. This CENP-B dimer configuration may be suitable for capturing two distant CENP-B boxes during centromeric heterochromatin formation. |
==About this Structure== | ==About this Structure== | ||
| - | 1UFI 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:// | + | 1UFI 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=1UFI OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kurumizaka, H.]] | [[Category: Kurumizaka, H.]] | ||
| - | [[Category: Park, S | + | [[Category: Park, S Y.]] |
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Tanaka, Y.]] | [[Category: Tanaka, Y.]] | ||
| - | [[Category: Tawaramoto, M | + | [[Category: Tawaramoto, M S.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: dimerization domain]] | [[Category: dimerization domain]] | ||
| Line 26: | Line 25: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:56 2008'' |
Revision as of 13:23, 21 February 2008
|
Crystal structure of the dimerization domain of human CENP-B
Overview
The human centromere protein B (CENP-B), a centromeric heterochromatin component, forms a homodimer that specifically binds to a distinct DNA sequence (the CENP-B box), which appears within every other alpha-satellite repeat. Previously, we determined the structure of the human CENP-B DNA-binding domain, CENP-B-(1-129), complexed with the CENP-B box DNA. In the present study, we determined the crystal structure of its dimerization domain (CENP-B-(540-599)), another functional domain of CENP-B, at 1.65-A resolution. CENP-B-(540-599) contains two alpha-helices, which are folded into an antiparallel configuration. The CENP-B-(540-599) dimer formed a symmetrical, antiparallel, four-helix bundle structure with a large hydrophobic patch in which 23 residues of one monomer form van der Waals contacts with the other monomer. In the CENP-B-(540-599) dimer, the N-terminal ends of CENP-B-(540-599) are oriented on opposite sides of the dimer. This CENP-B dimer configuration may be suitable for capturing two distant CENP-B boxes during centromeric heterochromatin formation.
About this Structure
1UFI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution., Tawaramoto MS, Park SY, Tanaka Y, Nureki O, Kurumizaka H, Yokoyama S, J Biol Chem. 2003 Dec 19;278(51):51454-61. Epub 2003 Sep 30. PMID:14522975
Page seeded by OCA on Thu Feb 21 15:23:56 2008
