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2LS7

High Definition Solution Structure of PED/PEA-15 Death Effector Domain

Summary for 2LS7
Entry DOI10.2210/pdb2ls7/pdb
Related1N3K
NMR InformationBMRB: 18412
DescriptorAstrocytic phosphoprotein PEA-15 (1 entity in total)
Functional Keywordssix helix bundle, death effector domain, death domain superfamily, apoptosis
Biological sourceMus musculus (mouse)
Cellular locationCytoplasm : Q62048
Total number of polymer chains1
Total formula weight10708.98
Authors
Twomey, E.C.,Wei, Y. (deposition date: 2012-04-20, release date: 2012-08-08, Last modification date: 2024-05-15)
Primary citationTwomey, E.C.,Wei, Y.
High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.
Biochem.Biophys.Res.Commun., 424:141-146, 2012
Cited by
PubMed Abstract: Death effector domain (DED) proteins constitute a subfamily of the large death domain superfamily that is primarily involved in apoptosis pathways. DED structures have characteristic side chain-side chain interactions among polar residues on the protein surface, forming a network of hydrogen bonds and salt bridges. The polar interaction network is functionally important in promoting protein-protein interactions by maintaining optimal side chain orientations. We have refined the solution DED structure of the PED/PEA-15 protein, a representative member of DED subfamily, using traditional NMR restraints with the addition of residual dipolar coupling (RDC) restraints from two independent alignment media, and employed the explicit solvent refinement protocol. The newly refined DED structure of PED/PEA-15 possesses higher structural quality as indicated by WHAT IF Z-scores, with most significant improvement in the backbone conformation normality quality factor. This higher quality DED structure of PED/PEA-15 leads to the identification of a number of key polar side chain interactions, which are not typically observed in NMR protein structures. The elucidation of polar side chain interactions is a key step towards the understanding of protein-protein interactions involving the death domain superfamily. The NMR structures with extensive details of protein structural features are thereby termed high-definition (HD) NMR structures.
PubMed: 22732408
DOI: 10.1016/j.bbrc.2012.06.091
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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