This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2l23

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

NMR structure of the ACID (ACtivator Interacting Domain) of the human mediator Med25 protein

Structural highlights

2l23 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MED25_HUMAN Charcot-Marie-Tooth disease type 2B2. The disease is caused by mutations affecting the gene represented in this entry.^[1]

Function

MED25_HUMAN 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 preinitiation complex with RNA polymerase II and the general transcription factors. Required for RARA/RXRA-mediated transcription.^[2] ^[3] ^[4]

Publication Abstract from PubMed

MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts with VP16 through a central MED25 PTOV (Prostate tumour overexpressed)/ACID (Activator interacting domain) domain of unknown structure. As a first step towards understanding the mechanism of recruitment of transactivation domains by MED25, we report here the NMR structure of the MED25 ACID domain. The domain architecture consists of a closed beta-barrel with seven strands (Beta1-Beta7) and three alpha-helices (H1-H3), an architecture showing similarities to that of the SPOC (Spen paralog and ortholog C-terminal domain) domain-like superfamily. Preliminary NMR chemical shift mapping showed that VP16 H2 (VP16C) interacts with MED25 ACID through one face of the beta-barrel, defined by strands B4-B7-B6.

NMR structure of the human Mediator MED25 ACID domain.,Bontems F, Verger A, Dewitte F, Lens Z, Baert JL, Ferreira E, Launoit YD, Sizun C, Guittet E, Villeret V, Monte D J Struct Biol. 2010 Oct 23. PMID:20974256^[5]

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

References

↑ Leal A, Huehne K, Bauer F, Sticht H, Berger P, Suter U, Morera B, Del Valle G, Lupski JR, Ekici A, Pasutto F, Endele S, Barrantes R, Berghoff C, Berghoff M, Neundorfer B, Heuss D, Dorn T, Young P, Santolin L, Uhlmann T, Meisterernst M, Sereda MW, Stassart RM, Meyer zu Horste G, Nave KA, Reis A, Rautenstrauss B. Identification of the variant Ala335Val of MED25 as responsible for CMT2B2: molecular data, functional studies of the SH3 recognition motif and correlation between wild-type MED25 and PMP22 RNA levels in CMT1A animal models. Neurogenetics. 2009 Oct;10(4):275-87. doi: 10.1007/s10048-009-0183-3. Epub 2009, Mar 17. PMID:19290556 doi:http://dx.doi.org/10.1007/s10048-009-0183-3
↑ Mittler G, Stuhler T, Santolin L, Uhlmann T, Kremmer E, Lottspeich F, Berti L, Meisterernst M. A novel docking site on Mediator is critical for activation by VP16 in mammalian cells. EMBO J. 2003 Dec 15;22(24):6494-504. PMID:14657022 doi:http://dx.doi.org/10.1093/emboj/cdg619
↑ Yang F, DeBeaumont R, Zhou S, Naar AM. The activator-recruited cofactor/Mediator coactivator subunit ARC92 is a functionally important target of the VP16 transcriptional activator. Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2339-44. PMID:14983011
↑ Lee HK, Park UH, Kim EJ, Um SJ. MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid receptor activation. EMBO J. 2007 Aug 8;26(15):3545-57. Epub 2007 Jul 19. PMID:17641689 doi:http://dx.doi.org/7601797
↑ Bontems F, Verger A, Dewitte F, Lens Z, Baert JL, Ferreira E, Launoit YD, Sizun C, Guittet E, Villeret V, Monte D. NMR structure of the human Mediator MED25 ACID domain. J Struct Biol. 2010 Oct 23. PMID:20974256 doi:10.1016/j.jsb.2010.10.011

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l23"

@@ Line 1: / Line 1: @@
 ==NMR structure of the ACID (ACtivator Interacting Domain) of the human mediator Med25 protein==
-<StructureSection load='2l23' size='340' side='right'caption='[[2l23]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l23' size='340' side='right'caption='[[2l23]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L23 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L23 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACID1, ARC92, MED25, PTOV2, TCBAP0758 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l23 OCA], [https://pdbe.org/2l23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l23 RCSB], [https://www.ebi.ac.uk/pdbsum/2l23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l23 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/MED25_HUMAN MED25_HUMAN]] Charcot-Marie-Tooth disease type 2B2. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:19290556</ref>
+[https://www.uniprot.org/uniprot/MED25_HUMAN MED25_HUMAN] Charcot-Marie-Tooth disease type 2B2. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:19290556</ref>
 == Function ==
-[[https://www.uniprot.org/uniprot/MED25_HUMAN MED25_HUMAN]] 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 preinitiation complex with RNA polymerase II and the general transcription factors. Required for RARA/RXRA-mediated transcription.<ref>PMID:14657022</ref> <ref>PMID:14983011</ref> <ref>PMID:17641689</ref>
+[https://www.uniprot.org/uniprot/MED25_HUMAN MED25_HUMAN] 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 preinitiation complex with RNA polymerase II and the general transcription factors. Required for RARA/RXRA-mediated transcription.<ref>PMID:14657022</ref> <ref>PMID:14983011</ref> <ref>PMID:17641689</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bontems, F]]
+[[Category: Bontems F]]
-[[Category: Dewitte, F]]
+[[Category: Dewitte F]]
-[[Category: Monte, D]]
+[[Category: Monte D]]
-[[Category: Villeret, V]]
+[[Category: Villeret V]]
-[[Category: Human mediator complex]]
-[[Category: Pancreatic tumor overexpressed domain]]
-[[Category: Transcription]]

2l23

From Proteopedia

Current revision

NMR structure of the ACID (ACtivator Interacting Domain) of the human mediator Med25 protein

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox