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5ht6

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Revision as of 08:31, 27 May 2020

Crystal structure of the SET domain of the human MLL5 methyltransferase

Structural highlights

5ht6 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	KMT2E, MLL5 (HUMAN)
Activity:	Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KMT2E_HUMAN] Histone methyltransferase that specifically mono- and dimethylates 'Lys-4' of histone H3 (H3K4me1 and H3K4me2). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation. Plays an essential role in retinoic-acid-induced granulopoiesis by acting as a coactivator of RAR-alpha (RARA) in target gene promoters. Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages. Required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells. Overexpression inhibits cell cycle progression, while knockdown induces cell cycle arrest at both the G1 and G2/M phases. Isoform NKp44L: Cellular ligand for NCR2/NKp44, may play a role as a danger signal in cytotoxicity and NK-cell-mediated innate immunity.

Publication Abstract from PubMed

Mixed Lineage Leukemia 5 (MLL5) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. Chromatin binding is ensured by its plant homeodomain (PHD) through a direct interaction with the N-terminus of histone H3 (H3). In addition, MLL5 contains a Su(var)3-9, Enhancer of zeste, Trithorax (SET) domain, a protein module that usually displays histone lysine methyltransferase activity. We report here the crystal structure of the unliganded SET domain of human MLL5 at 2.1 A resolution. Although it shows most of the canonical features of other SET domains, both the lack of key residues and the presence in the SET-I subdomain of an unusually large loop preclude the interaction of MLL5 SET with its cofactor and substrate. Accordingly, we show that MLL5 is devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptides. Hence, the three dimensional structure of MLL5 SET domain unveils the structural basis for its lack of methyltransferase activity and suggests a new regulatory mechanism.

The Human Mixed Lineage Leukemia 5 (MLL5), a Sequentially and Structurally Divergent SET Domain-Containing Protein with No Intrinsic Catalytic Activity.,Mas-Y-Mas S, Barbon M, Teyssier C, Demene H, Carvalho JE, Bird LE, Lebedev A, Fattori J, Schubert M, Dumas C, Bourguet W, le Maire A PLoS One. 2016 Nov 3;11(11):e0165139. doi: 10.1371/journal.pone.0165139., eCollection 2016. PMID:27812132^[1]

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

References

↑ Mas-Y-Mas S, Barbon M, Teyssier C, Demene H, Carvalho JE, Bird LE, Lebedev A, Fattori J, Schubert M, Dumas C, Bourguet W, le Maire A. The Human Mixed Lineage Leukemia 5 (MLL5), a Sequentially and Structurally Divergent SET Domain-Containing Protein with No Intrinsic Catalytic Activity. PLoS One. 2016 Nov 3;11(11):e0165139. doi: 10.1371/journal.pone.0165139., eCollection 2016. PMID:27812132 doi:http://dx.doi.org/10.1371/journal.pone.0165139

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ht6"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the SET domain of the human MLL5 methyltransferase==
-<StructureSection load='5ht6' size='340' side='right' caption='[[5ht6]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
+<StructureSection load='5ht6' size='340' side='right'caption='[[5ht6]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ht6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HT6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ht6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HT6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HT6 FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KMT2E, MLL5 ([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=5ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ht6 OCA], [http://pdbe.org/5ht6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ht6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ht6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ht6 ProSAT]</span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ht6 OCA], [http://pdbe.org/5ht6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ht6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ht6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ht6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5ht6" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
 == References ==
 <references/>
@@ Line 23: / Line 27: @@
 </StructureSection>
 [[Category: Histone-lysine N-methyltransferase]]
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Dumas, C]]
 [[Category: Lebedev, A]]

5ht6

From Proteopedia

Revision as of 08:31, 27 May 2020

Crystal structure of the SET domain of the human MLL5 methyltransferase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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