2lkm | pdb_00002lkm

Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology

spinqualitylabelsall models 2lkm, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lkm is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. Activity: Glucokinase, with EC number 2.7.1.2 Publication Abstract from PubMed MRG15 is a member of the mortality family of transcription factors that targets a wide variety of multiprotein complexes involved in transcription regulation, DNA repair, and alternative splicing to chromatin. The structure of the apo-MRG15 MRG domain implicated in interactions with diverse proteins has been described, but not in complex with any of its targets. Here, we structurally and functionally characterize the interaction between MRG15 and Pf1, two constitutively associated subunits of the histone deacetylase-associated Rpd3S/Sin3S corepressor complex. The MRG domain adopts a structure reminiscent of the apo state, whereas the Pf1 MRG-binding domain engages two discrete hydrophobic surfaces on the MRG domain via a bipartite motif comprising an alpha-helix and a segment in an extended conformation, both of which are critical for high-affinity interactions. Multiple MRG15 interactors share an FxLP motif in the extended segment, but equivalent sequence/helical motifs are not readily evident, implying potential diversity in MRG-recognition mechanisms. Structural basis for molecular interactions involving MRG domains: implications in chromatin biology.,Xie T, Graveline R, Kumar GS, Zhang Y, Krishnan A, David G, Radhakrishnan I Structure. 2012 Jan 11;20(1):151-60. PMID:22244764 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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