3rsn
From Proteopedia
Crystal Structure of the N-terminal region of Human Ash2L
Structural highlights
Function[ASH2L_HUMAN] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.[1] [2] Publication Abstract from PubMedAsh2L is a core component of the MLL family histone methyltransferases and has an important role in regulating the methylation of histone H3 on lysine 4. Here, we report the crystal structure of the N-terminal domain of Ash2L and reveal a new function of Ash2L. The structure shows that Ash2L contains an atypical PHD finger that does not have histone tail-binding activity. Unexpectedly, the structure shows a previously unrecognized winged-helix motif that directly binds to DNA. The DNA-binding-deficient mutants of Ash2L reduced Ash2L localization to the HOX locus. Strikingly, a single mutation in Ash2L(WH) (K131A) breaks the chromatin domain boundary, suggesting that Ash2L also has a role in chromosome demarcation. Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding.,Chen Y, Wan B, Wang KC, Cao F, Yang Y, Protacio A, Dou Y, Chang HY, Lei M EMBO Rep. 2011 Jun 10. doi: 10.1038/embor.2011.101. PMID:21660059[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Human | Large Structures | Cao, F | Chang, H Y | Chen, Y | Dou, Y | Lei, M | Protacio, A | Wan, B | Wang, K C | Yang, Y | Dna binding | Histone methyltransferase | Phd domain | Transcription | Winged helix domain
