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3Q6S

The crystal structure of the heterochromatin protein 1 beta chromoshadow domain complexed with a peptide from Shugoshin 1

Summary for 3Q6S
Entry DOI10.2210/pdb3q6s/pdb
DescriptorChromobox protein homolog 1, Shugoshin-like 1 (3 entities in total)
Functional Keywordsincenp, heterochromatin, centromere, cell cycle
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: P83916 Q5FBB7
Total number of polymer chains6
Total formula weight40241.21
Authors
Brautigam, C.A.,Chaudhary, J.,Yu, H. (deposition date: 2011-01-03, release date: 2011-12-14, Last modification date: 2024-02-21)
Primary citationKang, J.,Chaudhary, J.,Dong, H.,Kim, S.,Brautigam, C.A.,Yu, H.
Mitotic centromeric targeting of HP1 and its binding to Sgo1 are dispensable for sister-chromatid cohesion in human cells.
Mol Biol Cell, 22:1181-1190, 2011
Cited by
PubMed Abstract: Human Shugoshin 1 (Sgo1) protects centromeric sister-chromatid cohesion during prophase and prevents premature sister-chromatid separation. Heterochromatin protein 1 (HP1) has been proposed to protect centromeric sister-chromatid cohesion by directly targeting Sgo1 to centromeres in mitosis. Here we show that HP1α is targeted to mitotic centromeres by INCENP, a subunit of the chromosome passenger complex (CPC). Biochemical and structural studies show that both HP1-INCENP and HP1-Sgo1 interactions require the binding of the HP1 chromo shadow domain to PXVXL/I motifs in INCENP or Sgo1, suggesting that the INCENP-bound, centromeric HP1α is incapable of recruiting Sgo1. Consistently, a Sgo1 mutant deficient in HP1 binding is functional in centromeric cohesion protection and localizes normally to centromeres in mitosis. By contrast, INCENP or Sgo1 mutants deficient in HP1 binding fail to localize to centromeres in interphase. Therefore, our results suggest that HP1 binding by INCENP or Sgo1 is dispensable for centromeric cohesion protection during mitosis of human cells, but might regulate yet uncharacterized interphase functions of CPC or Sgo1 at the centromeres.
PubMed: 21346195
DOI: 10.1091/mbc.E11-01-0009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.93 Å)
Structure validation

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