2pqw
From Proteopedia
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Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form
Overview
Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4, peptides dimethylated on Lys20 (H4K20me2) show that only the second of the, three MBT repeats can bind mono- and dimethylated histone peptides. Its, binding pocket has similarities to that of 53BP1 and is able to recognize, the degree of histone lysine methylation. An unexpected mode of, peptide-mediated dimerization suggests a possible mechanism for chromatin, compaction by L3MBTL1.
About this Structure
2PQW is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
L3MBTL1 recognition of mono- and dimethylated histones., Min J, Allali-Hassani A, Nady N, Qi C, Ouyang H, Liu Y, Mackenzie F, Vedadi M, Arrowsmith CH, Nat Struct Mol Biol. 2007 Nov 18;. PMID:18026117
Page seeded by OCA on Wed Jan 23 11:31:27 2008
Categories: Homo sapiens | Single protein | Allali-Hassani, A. | Arrowsmith, C.H. | Bochkarev, A. | Crombet, L. | Edwards, A.M. | Herzanych, N. | Kozieradzki, I. | Liu, Y. | Loppnau, P. | Mackenzie, F. | Min, J.R. | Ouyang, H. | SGC, Structural.Genomics.Consortium. | Sundstrom, M. | Vedadi, M. | Weigelt, J. | ACT | L(3)mbt-like protein | Sgc | Structural genomics | Structural genomics consortium | Transcription
