5odd

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<StructureSection load='5odd' size='340' side='right' caption='[[5odd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='5odd' size='340' side='right' caption='[[5odd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5odd]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2mzo 2mzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ODD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ODD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5odd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2mzo 2mzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ODD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ODD FirstGlance]. <br>
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</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=5odd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5odd OCA], [http://pdbe.org/5odd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5odd RCSB], [http://www.ebi.ac.uk/pdbsum/5odd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5odd ProSAT]</span></td></tr>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MED26, ARC70, CRSP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=5odd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5odd OCA], [http://pdbe.org/5odd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5odd RCSB], [http://www.ebi.ac.uk/pdbsum/5odd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5odd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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MED26 is a subunit of Mediator, a large complex central to the regulation of gene transcription by RNA Polymerase II. MED26 plays a role in the switch between the initiation and elongation phases of RNA Polymerase II-mediated transcription process. Regulation of these steps requires successive binding of MED26 N-terminal domain (NTD) to TATA-binding protein-associated factor 7 (TAF7) and Eleven-nineteen lysine-rich in leukemia-Associated Factor 1 (EAF1). In order to investigate the mechanism of regulation by MED26, MED26-NTD structure was solved by NMR, revealing a 4-helix bundle. EAF1 (239-268) and TAF7 (205-235) peptide interactions were both mapped to the same groove formed by H3 and H4 helices of MED26-NTD. Both interactions are characterized by dissociation constants in the 10-muM range. Further experiments revealed a folding-upon-binding mechanism that leads to the formation of EAF1 (N247-S260) and TAF7 (L214-S227) helices. Chemical shift perturbations and nuclear Overhauser enhancement contacts support the involvement of residues I222/F223 in anchoring TAF7 helix to a hydrophobic pocket of MED26-NTD, including residues L48, W80 and I84. In addition, Ala mutations of charged residues located in the C-terminal disordered part of TAF7 and EAF1 peptides affected the binding, with a loss of affinity characterized by a 10-time increase of dissociation constants. A structural model of MED26-NTD/TAF7 complex shows bi-partite components, combining ordered and disordered segments, as well as hydrophobic and electrostatic contributions to the binding. This study provides molecular detail that will help to decipher the mechanistic basis for the initiation to elongation switch-function mediated by MED26-NTD.
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MED26 is a subunit of the Mediator, a very large complex involved in regulation of gene transcription by RNA Polymerase II. MED26 regulates the switch between initiation and elongation phases of the transcription. This function requires interaction of its N-terminal domain (NTD) with several protein partners implicated in transcriptional regulation. Molecular details of the structure and interaction mode of MED26 NTD would improve understanding of this complex regulation. As a first step towards structural characterization, sequence specific (1)H, (13)C and (15)N assignments for MED26 NTD was performed based on Nuclear Magnetic Resonance spectroscopy. TALOS+ analysis of the chemical shifts data revealed a domain solely composed of helices. Assignments will be further used to solve NMR structure and dynamics of MED26 NTD and investigate the molecular details of its interaction with protein partners.
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Solution Structure of the N-Terminal Domain of Mediator Subunit MED26 and Molecular Characterization of Its Interaction with EAF1 and TAF7.,Lens Z, Cantrelle FX, Peruzzini R, Hanoulle X, Dewitte F, Ferreira E, Baert JL, Monte D, Aumercier M, Villeret V, Verger A, Landrieu I J Mol Biol. 2017 Oct 13;429(20):3043-3055. doi: 10.1016/j.jmb.2017.09.001. Epub, 2017 Sep 9. PMID:28893534<ref>PMID:28893534</ref>
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1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26.,Peruzzini R, Lens Z, Verger A, Dewitte F, Ferreira E, Baert JL, Villeret V, Landrieu I, Cantrelle FX Biomol NMR Assign. 2016 Apr;10(1):233-6. doi: 10.1007/s12104-016-9673-z. Epub, 2016 Feb 9. PMID:26861138<ref>PMID:26861138</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Cantrelle, F X]]
[[Category: Cantrelle, F X]]
[[Category: Dewitte, F]]
[[Category: Dewitte, F]]

Revision as of 06:05, 11 July 2018

HUMAN MED26 N-TERMINAL DOMAIN (1-92)

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