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

Summary for 2L6U

• Entry DOI: 10.2210/pdb2l6u/pdb
• NMR Information: BMRB: 17323
• Descriptor: Mediator complex subunit MED25 (1 entity in total)
• Functional Keywords: structural genomics, northeast structural genomics consortium (nesg), psi-biology, protein structure initiative, arc92, acid, ptov, transcription
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18637.62

Authors

Eletsky, A.,Ryuechan, W.T.,Sukumaran, D.K.,Shastry, R.,Ciccosanti, C.,Janjua, H.,Acton, T.B.,Xiao, R.,Everett, J.K.,Montelione, G.T.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2010-11-24, release date: 2011-01-12, Last modification date: 2024-05-15)

Primary citation

Eletsky, A.,Ruyechan, W.T.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Szyperski, T.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
J.Struct.Funct.Genom., 12:159-166, 2011

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.

PubMed: 21785987
DOI: 10.1007/s10969-011-9115-1

Experimental method

SOLUTION NMR