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3F70

Crystal structure of L3MBTL2-H4K20me1 complex

Replaces:  3DBB
Summary for 3F70
Entry DOI10.2210/pdb3f70/pdb
Related3CEY
DescriptorLethal(3)malignant brain tumor-like 2 protein, N-METHYL-LYSINE (3 entities in total)
Functional Keywordsmbt, chromatin regulator, metal-binding, nucleus, transcription, transcription regulation, zinc-finger, transcription regulator, structural genomics, structural genomics consortium, sgc, phosphoprotein
Biological sourceHomo sapiens (human)
Cellular locationNucleus : Q969R5
Total number of polymer chains2
Total formula weight104614.45
Authors
Primary citationGuo, Y.,Nady, N.,Qi, C.,Allali-Hassani, A.,Zhu, H.,Pan, P.,Adams-Cioaba, M.A.,Amaya, M.F.,Dong, A.,Vedadi, M.,Schapira, M.,Read, R.J.,Arrowsmith, C.H.,Min, J.
Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2.
Nucleic Acids Res., 37:2204-2210, 2009
Cited by
PubMed Abstract: The MBT repeat has been recently identified as a key domain capable of methyl-lysine histone recognition. Functional work has pointed to a role for MBT domain-containing proteins in transcriptional repression of developmental control genes such as Hox genes. In this study, L3MBTL2, a human homolog of Drosophila Sfmbt critical for Hox gene silencing, is demonstrated to preferentially recognize lower methylation states of several histone-derived peptides through its fourth MBT repeat. High-resolution crystallographic analysis of the four MBT repeats of this protein reveals its unique asymmetric rhomboid architecture, as well as binding mechanism, which preclude the interaction of the first three MBT repeats with methylated peptides. Structural elucidation of an L3MBTL2-H4K20me1 complex and comparison with other MBT-histone peptide complexes also suggests that an absence of distinct surface contours surrounding the methyl-lysine-binding pocket may underlie the lack of sequence specificity observed for members of this protein family.
PubMed: 19233876
DOI: 10.1093/nar/gkp086
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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