2L6U

Solution NMR Structure of Med25(391-543) Comprising the Activator-Interacting Domain (ACID) of Human Mediator Subuniti 25. Northeast Structural Genomics Consortium Target HR6188A


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.7 of the entry. See complete history


Literature

Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.

Eletsky, A.Ruyechan, W.T.Xiao, R.Acton, T.B.Montelione, G.T.Szyperski, T.

(2011) J Struct Funct Genomics 12: 159-166

  • DOI: https://doi.org/10.1007/s10969-011-9115-1
  • Primary Citation of Related Structures:  
    2L6U

  • PubMed Abstract: 

    The solution NMR structure of protein MED25(391-543), comprising the activator interacting domain (ACID) of subunit 25 of the human mediator, is presented along with the measurement of polypeptide backbone heteronuclear 15N-{1H} NOEs to identify fast internal motional modes. This domain interacts with the acidic transactivation domains of Herpes simplex type 1 (HSV-1) protein VP16 and the Varicella-zoster virus (VZV) major transactivator protein IE62, which initiate transcription of viral genes. The structure is similar to the β-barrel domains of the human protein Ku and the SPOC domain of human protein SHARP, and provides a starting point to understand the structural biology of initiation of HSV-1 and VZV gene activation. Homology models built for the two ACID domains of the prostate tumor overexpressed (PTOV1) protein using the structure of MED25(391-543) as a template suggest that differential biological activities of the ACID domains in MED25 and PTOV1 arise from modulation of quite similar protein-protein interactions by variable residues grouped around highly conserved charged surface areas.


  • Organizational Affiliation

    Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Mediator complex subunit MED25163Homo sapiensMutation(s): 0 
Gene Names: MED25
UniProt & NIH Common Fund Data Resources
Find proteins for Q71SY5 (Homo sapiens)
Explore Q71SY5 
Go to UniProtKB:  Q71SY5
PHAROS:  Q71SY5
GTEx:  ENSG00000104973 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ71SY5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2011-01-12
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2011-09-28
    Changes: Database references
  • Version 1.3: 2012-02-22
    Changes: Structure summary
  • Version 1.4: 2020-02-05
    Changes: Data collection, Database references, Other
  • Version 1.5: 2021-08-18
    Changes: Database references, Experimental preparation
  • Version 1.6: 2023-06-14
    Changes: Other
  • Version 1.7: 2024-05-15
    Changes: Data collection, Database references