3G36

Crystal structure of the human DPY-30-like C-terminal domain

Summary for 3G36

• Entry DOI: 10.2210/pdb3g36/pdb
• Descriptor: Protein dpy-30 homolog, (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (6 entities in total)
• Functional Keywords: x-type four-helix bundle, nucleus, nuclear protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 25813.59

Authors

Wang, X.,Lou, Z.,Bartlam, M.,Rao, Z. (deposition date: 2009-02-02, release date: 2009-06-30, Last modification date: 2024-10-30)

Primary citation

Wang, X.,Lou, Z.,Dong, X.,Yang, W.,Peng, Y.,Yin, B.,Gong, Y.,Yuan, J.,Zhou, W.,Bartlam, M.,Peng, X.,Rao, Z.
Crystal structure of the C-terminal domain of human DPY-30-like protein: A component of the histone methyltransferase complex
J.Mol.Biol., 390:530-537, 2009

PubMed Abstract: The conserved DPY-30 is an essential component of the dosage compensation complex that balances the X-linked gene expression by regulation of the complex formation in Caenorhabditis elegans. The human DPY-30-like protein (DPY-30L) homolog is a conserved member of certain histone methyltransferase (HMT) complexes. In the human MLL1 (mixed-lineage leukemia-1) HMT complex, DPY-30L binds to the BRE2 homolog ASH2L in order to regulate histone 3-lysine 4 trimethylation. We have determined the 1.2-A crystal structure of the human DPY-30L C-terminal domain (DPY-30L(C)). The DPY-30L(C) structure, harboring the conserved DPY-30 motif, is composed of two alpha-helices linked by a sharp loop and forms a typical X-type four-helix bundle required for dimer formation. DPY-30L(C) dimer formation is largely mediated by an extensive hydrophobic interface with some additional polar interactions. The oligomerization of DPY-30L(C) in solution, together with its reported binding to ASH2L, leads us to propose that the hydrophobic surface of the dimer may provide a platform for interaction with ASH2L in the MLL1 HMT complex.

PubMed: 19481096
DOI: 10.1016/j.jmb.2009.05.061

Experimental method

X-RAY DIFFRACTION (1.2 Å)