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5yhu

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Revision as of 07:35, 4 July 2018

Crystal structure of the DNA-binding domain of human myelin-gene regulatory factor

Structural highlights

5yhu 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:	MYRF, C11orf9, KIAA0954, MRF (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYRF_HUMAN] Myelin regulatory factor: Constitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor, N-terminal component that specifically activates transcription of central nervous system (CNS) myelin genes (PubMed:23966832).^[1] Myelin regulatory factor, C-terminal: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage.^[2] Myelin regulatory factor, N-terminal: Transcription factor that specifically activates expression of myelin genes such as MBP, MOG, MAG, DUSP15 and PLP1 during oligodendrocyte (OL) maturation, thereby playing a central role in oligodendrocyte maturation and CNS myelination. Specifically recognizes and binds DNA sequence 5'-CTGGYAC-3' in the regulatory regions of myelin-specific genes and directly activates their expression. Not only required during oligodendrocyte differentiation but is also required on an ongoing basis for the maintenance of expression of myelin genes and for the maintenance of a mature, viable oligodendrocyte phenotype (PubMed:23966832).^[3]

Publication Abstract from PubMed

Myelin-gene regulatory factor (MYRF) is a membrane-bound transcription factors, which is responsible for the differentiation of oligodendrocytes and myelination of central nervous system. Followed by a self-cleavage by the intramolecular chaperone auto-processing (ICA) domain, DNA-binding domain (DBD) of MYRF is released from the endoplasmic reticulum (ER) and was then translocated to the nucleus to regulate gene expression. In present work, we have solved the crystal structure of the human MYRF-DBD to 1.85-A resolution. It exhibits a typical s-type Ig-fold and packs as symmetric trimeric form in the crystal via hydrogen-bond networks in three regions. Accordingly, we identified a couple of key residues on MYRF-DBD, which might play important roles in DNA-binding, in particular Arg521 on its C-terminal tail. The R521A mutant of DBD showed only 17% affinity to dsDNA targets compared to wild-type DBD. Then we built a plausible protein-DNA binding model of MYRF-DBD, which will help to elucidate its mechanism in DNA-binding and transcriptional regulation.

Structure of the DNA-binding domain of human myelin-gene regulatory factor reveals its potential protein-DNA recognition mode.,Chen B, Zhu Y, Ye S, Zhang R J Struct Biol. 2018 May 2. pii: S1047-8477(18)30115-1. doi:, 10.1016/j.jsb.2018.04.007. PMID:29729323^[4]

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

References

↑ Li Z, Park Y, Marcotte EM. A Bacteriophage tailspike domain promotes self-cleavage of a human membrane-bound transcription factor, the myelin regulatory factor MYRF. PLoS Biol. 2013;11(8):e1001624. doi: 10.1371/journal.pbio.1001624. Epub 2013 Aug , 13. PMID:23966832 doi:http://dx.doi.org/10.1371/journal.pbio.1001624
↑ Li Z, Park Y, Marcotte EM. A Bacteriophage tailspike domain promotes self-cleavage of a human membrane-bound transcription factor, the myelin regulatory factor MYRF. PLoS Biol. 2013;11(8):e1001624. doi: 10.1371/journal.pbio.1001624. Epub 2013 Aug , 13. PMID:23966832 doi:http://dx.doi.org/10.1371/journal.pbio.1001624
↑ Li Z, Park Y, Marcotte EM. A Bacteriophage tailspike domain promotes self-cleavage of a human membrane-bound transcription factor, the myelin regulatory factor MYRF. PLoS Biol. 2013;11(8):e1001624. doi: 10.1371/journal.pbio.1001624. Epub 2013 Aug , 13. PMID:23966832 doi:http://dx.doi.org/10.1371/journal.pbio.1001624
↑ Chen B, Zhu Y, Ye S, Zhang R. Structure of the DNA-binding domain of human myelin-gene regulatory factor reveals its potential protein-DNA recognition mode. J Struct Biol. 2018 May 2. pii: S1047-8477(18)30115-1. doi:, 10.1016/j.jsb.2018.04.007. PMID:29729323 doi:http://dx.doi.org/10.1016/j.jsb.2018.04.007

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='5yhu' size='340' side='right' caption='[[5yhu]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5yhu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YHU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5yhu]] 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=5YHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YHU FirstGlance]. <br>
-</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=5yhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yhu OCA], [http://pdbe.org/5yhu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yhu RCSB], [http://www.ebi.ac.uk/pdbsum/5yhu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yhu ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYRF, C11orf9, KIAA0954, MRF ([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=5yhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yhu OCA], [http://pdbe.org/5yhu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yhu RCSB], [http://www.ebi.ac.uk/pdbsum/5yhu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yhu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Chen, B]]
 [[Category: Ye, S]]

5yhu

From Proteopedia

Revision as of 07:35, 4 July 2018

Crystal structure of the DNA-binding domain of human myelin-gene regulatory factor

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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