2RJC

Crystal structure of L3MBTL1 protein in complex with MES

Summary for 2RJC

• Entry DOI: 10.2210/pdb2rjc/pdb
• Related: 2PQW 2RJD 2RJE 2RJF
• Descriptor: Lethal(3)malignant brain tumor-like protein, SULFATE ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: l(3)mbt-like protein, structural genomics, structural genomics consortium, sgc, transcription, chromatin regulator, dna-binding, metal-binding, nucleus, repressor, transcription regulation, zinc-finger
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9Y468
• Total number of polymer chains: 3
• Total formula weight: 114905.37

Authors

Allali-Hassani, A.,Liu, Y.,Herzanych, N.,Ouyang, H.,Mackenzie, F.,Crombet, L.,Loppnau, P.,Kozieradzki, I.,Vedadi, M.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.R.,Structural Genomics Consortium (SGC) (deposition date: 2007-10-14, release date: 2007-10-30, Last modification date: 2023-08-30)

Primary citation

Min, J.,Allali-Hassani, A.,Nady, N.,Qi, C.,Ouyang, H.,Liu, Y.,MacKenzie, F.,Vedadi, M.,Arrowsmith, C.H.
L3MBTL1 recognition of mono- and dimethylated histones.
Nat.Struct.Mol.Biol., 14:1229-1230, 2007

PubMed Abstract: 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.

PubMed: 18026117
DOI: 10.1038/nsmb1340

Experimental method

X-RAY DIFFRACTION (2 Å)