|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal structure of the dimerization domain of human CENP-B== | | ==Crystal structure of the dimerization domain of human CENP-B== |
| - | <StructureSection load='1ufi' size='340' side='right' caption='[[1ufi]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='1ufi' size='340' side='right'caption='[[1ufi]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ufi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UFI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ufi]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UFI FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CENPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ufi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ufi OCA], [http://pdbe.org/1ufi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ufi RCSB], [http://www.ebi.ac.uk/pdbsum/1ufi PDBsum], [http://www.topsan.org/Proteins/RSGI/1ufi TOPSAN]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ufi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ufi OCA], [https://pdbe.org/1ufi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ufi RCSB], [https://www.ebi.ac.uk/pdbsum/1ufi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ufi ProSAT], [https://www.topsan.org/Proteins/RSGI/1ufi TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CENPB_HUMAN CENPB_HUMAN]] Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes. | + | [https://www.uniprot.org/uniprot/CENPB_HUMAN CENPB_HUMAN] Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 19: |
Line 20: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Centromere protein|Centromere protein]] | + | *[[Centromere protein 3D structure|Centromere protein 3D structure]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kurumizaka, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Park, S Y]] | + | [[Category: Kurumizaka H]] |
| - | [[Category: Structural genomic]] | + | [[Category: Park S-Y]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Tawaramoto, M S]] | + | [[Category: Tawaramoto MS]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Dimerization domain]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Salt bridge]]
| + | |
| Structural highlights
Function
CENPB_HUMAN Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tawaramoto MS, Park SY, Tanaka Y, Nureki O, Kurumizaka H, Yokoyama S. Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution. J Biol Chem. 2003 Dec 19;278(51):51454-61. Epub 2003 Sep 30. PMID:14522975 doi:http://dx.doi.org/10.1074/jbc.M310388200
|
