6h02: Difference between revisions

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'''Unreleased structure'''


The entry 6h02 is ON HOLD  until Jan 06 2020
==Crystal structure of human Mediator subunit MED23==
<StructureSection load='6h02' size='340' side='right'caption='[[6h02]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6h02]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H02 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6h02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h02 OCA], [https://pdbe.org/6h02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h02 RCSB], [https://www.ebi.ac.uk/pdbsum/6h02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h02 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/MED23_HUMAN MED23_HUMAN] Autosomal recessive non-syndromic intellectual disability. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/MED23_HUMAN MED23_HUMAN] Required for transcriptional activation subsequent to the assembly of the pre-initiation complex (By similarity). Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling.<ref>PMID:10353252</ref> <ref>PMID:14759369</ref> <ref>PMID:16595664</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Mediator complex transduces regulatory information from enhancers to promoters and performs essential roles in the initiation of transcription in eukaryotes. Human Mediator comprises 26 subunits forming three modules termed Head, Middle and Tail. Here we present the 2.8 A crystal structure of MED23, the largest subunit from the human Tail module. The structure identifies 25 HEAT repeats-like motifs organized into 5 alpha-solenoids. MED23 adopts an arch-shaped conformation, with an N-terminal domain (Nter) protruding from a large core region. In the core four solenoids, motifs wrap on themselves, creating triangular-shaped structural motifs on both faces of the arch, with extended grooves propagating through the interfaces between the solenoid motifs. MED23 is known to interact with several specific transcription activators and is involved in splicing, elongation, and post-transcriptional events. The structure rationalizes previous biochemical observations and paves the way for improved understanding of the cross-talk between Mediator and transcriptional activators.


Authors:  
Crystal structure of human Mediator subunit MED23.,Monte D, Clantin B, Dewitte F, Lens Z, Rucktooa P, Pardon E, Steyaert J, Verger A, Villeret V Nat Commun. 2018 Aug 23;9(1):3389. doi: 10.1038/s41467-018-05967-y. PMID:30140054<ref>PMID:30140054</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6h02" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Mediator|Mediator]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Clantin B]]
[[Category: Monte D]]
[[Category: Villeret V]]

Latest revision as of 13:00, 23 October 2024

Crystal structure of human Mediator subunit MED23Crystal structure of human Mediator subunit MED23

Structural highlights

6h02 is a 2 chain structure with sequence from Homo sapiens and Lama glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MED23_HUMAN Autosomal recessive non-syndromic intellectual disability. The disease is caused by mutations affecting the gene represented in this entry.

Function

MED23_HUMAN Required for transcriptional activation subsequent to the assembly of the pre-initiation complex (By similarity). Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling.[1] [2] [3]

Publication Abstract from PubMed

The Mediator complex transduces regulatory information from enhancers to promoters and performs essential roles in the initiation of transcription in eukaryotes. Human Mediator comprises 26 subunits forming three modules termed Head, Middle and Tail. Here we present the 2.8 A crystal structure of MED23, the largest subunit from the human Tail module. The structure identifies 25 HEAT repeats-like motifs organized into 5 alpha-solenoids. MED23 adopts an arch-shaped conformation, with an N-terminal domain (Nter) protruding from a large core region. In the core four solenoids, motifs wrap on themselves, creating triangular-shaped structural motifs on both faces of the arch, with extended grooves propagating through the interfaces between the solenoid motifs. MED23 is known to interact with several specific transcription activators and is involved in splicing, elongation, and post-transcriptional events. The structure rationalizes previous biochemical observations and paves the way for improved understanding of the cross-talk between Mediator and transcriptional activators.

Crystal structure of human Mediator subunit MED23.,Monte D, Clantin B, Dewitte F, Lens Z, Rucktooa P, Pardon E, Steyaert J, Verger A, Villeret V Nat Commun. 2018 Aug 23;9(1):3389. doi: 10.1038/s41467-018-05967-y. PMID:30140054[4]

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

See Also

References

  1. Boyer TG, Martin ME, Lees E, Ricciardi RP, Berk AJ. Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein. Nature. 1999 May 20;399(6733):276-9. PMID:10353252 doi:http://dx.doi.org/10.1038/20466
  2. Mo X, Kowenz-Leutz E, Xu H, Leutz A. Ras induces mediator complex exchange on C/EBP beta. Mol Cell. 2004 Jan 30;13(2):241-50. PMID:14759369
  3. Baek HJ, Kang YK, Roeder RG. Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly. J Biol Chem. 2006 Jun 2;281(22):15172-81. Epub 2006 Apr 4. PMID:16595664 doi:M601983200
  4. Monte D, Clantin B, Dewitte F, Lens Z, Rucktooa P, Pardon E, Steyaert J, Verger A, Villeret V. Crystal structure of human Mediator subunit MED23. Nat Commun. 2018 Aug 23;9(1):3389. doi: 10.1038/s41467-018-05967-y. PMID:30140054 doi:http://dx.doi.org/10.1038/s41467-018-05967-y

6h02, resolution 2.80Å

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