2ri3
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(New page: 200px<br /><applet load="2ri3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ri3, resolution 2.0Å" /> '''Crystal structure of ...)
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Revision as of 09:45, 23 January 2008
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Crystal structure of the 3-MBT repeats from human L3MBTL1 with N358Q point mutation
Overview
Human L3MBTL1, which contains three malignant brain tumor (MBT) repeats, binds monomethylated and dimethylated lysines, but not trimethylated, lysines, in several histone sequence contexts. In crystal structures of, L3MBTL1 complexes, the monomethyl- and dimethyllysines insert into a, narrow and deep cavity of aromatic residue-lined pocket 2, while a proline, ring inserts into shallower pocket 1. We have also engineered a single Y, to E substitution within the aromatic cage of the BPTF PHD finger, resulting in a reversal of binding preference from trimethyl- to, dimethyllysine in an H3K4 sequence context. In both the "cavity insertion", (L3MBTL1) and "surface groove" (PHD finger) modes of methyllysine, recognition, a carboxylate group both hydrogen bonds and ion pairs to the, methylammonium proton. Our structural and binding studies of these two, modules provide insights into the molecular principles governing the, decoding of lysine methylation states, thereby highlighting a methylation, state-specific layer of histone mark readout impacting on epigenetic, regulation.
About this Structure
2RI3 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structural Basis for Lower Lysine Methylation State-Specific Readout by MBT Repeats of L3MBTL1 and an Engineered PHD Finger., Li H, Fischle W, Wang W, Duncan EM, Liang L, Murakami-Ishibe S, Allis CD, Patel DJ, Mol Cell. 2007 Nov 30;28(4):677-91. PMID:18042461
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