This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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
