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3R93

Crystal structure of the chromo domain of M-phase phosphoprotein 8 bound to H3K9Me3 peptide

Summary for 3R93
Entry DOI10.2210/pdb3r93/pdb
Related3LWE
DescriptorM-phase phosphoprotein 8, H3K9Me3 peptide, UNKNOWN ATOM OR ION, ... (4 entities in total)
Functional Keywordsepigenetics, cell cycle, m-phase, chromodomain, structural genomics, structural genomics consortium, sgc
Biological sourceHomo sapiens (human)
Cellular locationNucleus : Q99549
Total number of polymer chains8
Total formula weight35808.91
Authors
Li, J.,Li, Z.,Ruan, J.,Xu, C.,Tong, Y.,Pan, P.W.,Tempel, W.,Crombet, L.,Min, J.,Zang, J.,Structural Genomics Consortium (SGC) (deposition date: 2011-03-24, release date: 2011-04-06, Last modification date: 2023-09-13)
Primary citationLi, J.,Li, Z.,Ruan, J.,Xu, C.,Tong, Y.,Pan, P.W.,Tempel, W.,Crombet, L.,Min, J.,Zang, J.
Structural basis for specific binding of human MPP8 chromodomain to histone H3 methylated at lysine 9.
Plos One, 6:e25104-e25104, 2011
Cited by
PubMed Abstract: M-phase phosphoprotein 8 (MPP8) was initially identified to be a component of the RanBPM-containing large protein complex, and has recently been shown to bind to methylated H3K9 both in vivo and in vitro. MPP8 binding to methylated H3K9 is suggested to recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promote tumor cell motility and invasion. MPP8 contains a chromodomain in its N-terminus, which is used to bind the methylated H3K9.
PubMed: 22022377
DOI: 10.1371/journal.pone.0025104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.057 Å)
Structure validation

226707

数据于2024-10-30公开中

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