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3f70

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Revision as of 09:27, 25 October 2017

Crystal structure of L3MBTL2-H4K20me1 complex

Structural highlights

3f70 is a 2 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 3dbb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3cey
Gene:	L3MBTL2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LMBL2_HUMAN] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2.,Guo Y, Nady N, Qi C, Allali-Hassani A, Zhu H, Pan P, Adams-Cioaba MA, Amaya MF, Dong A, Vedadi M, Schapira M, Read RJ, Arrowsmith CH, Min J Nucleic Acids Res. 2009 Apr;37(7):2204-10. Epub 2009 Feb 20. PMID:19233876^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Guo Y, Nady N, Qi C, Allali-Hassani A, Zhu H, Pan P, Adams-Cioaba MA, Amaya MF, Dong A, Vedadi M, Schapira M, Read RJ, Arrowsmith CH, Min J. Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2. Nucleic Acids Res. 2009 Apr;37(7):2204-10. Epub 2009 Feb 20. PMID:19233876 doi:10.1093/nar/gkp086
↑ Guo Y, Nady N, Qi C, Allali-Hassani A, Zhu H, Pan P, Adams-Cioaba MA, Amaya MF, Dong A, Vedadi M, Schapira M, Read RJ, Arrowsmith CH, Min J. Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2. Nucleic Acids Res. 2009 Apr;37(7):2204-10. Epub 2009 Feb 20. PMID:19233876 doi:10.1093/nar/gkp086

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3f70"

@@ Line 1: / Line 1: @@
 ==Crystal structure of L3MBTL2-H4K20me1 complex==
 <StructureSection load='3f70' size='340' side='right' caption='[[3f70]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cey|3cey]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L3MBTL2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f70 OCA], [http://pdbe.org/3f70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f70 RCSB], [http://www.ebi.ac.uk/pdbsum/3f70 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f70 OCA], [http://pdbe.org/3f70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f70 RCSB], [http://www.ebi.ac.uk/pdbsum/3f70 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f70 ProSAT]</span></td></tr>
 </table>
 == Function ==

3f70

From Proteopedia

Revision as of 09:27, 25 October 2017

Crystal structure of L3MBTL2-H4K20me1 complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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