3DSH

Crystal structure of dimeric interferon regulatory factor 5 (IRF-5) transactivation domain

3DSH の概要

• エントリーDOI: 10.2210/pdb3dsh/pdb
• 分子名称: Interferon regulatory factor 5 (2 entities in total)
• 機能のキーワード: phosphoactivation induced dimerization, dna-binding, nucleus, transcription, transcription regulation, dna binding protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus: Q13568
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28595.84

構造登録者

Chen, W.,Lam, S.S.,Srinath, H.,Jiang, Z.,Correia, J.J.,Schiffer, C.,Fitzgerald, K.A.,Lin, K.,Royer Jr., W.E. (登録日: 2008-07-12, 公開日: 2008-10-07, 最終更新日: 2024-02-21)

主引用文献

Chen, W.,Lam, S.S.,Srinath, H.,Jiang, Z.,Correia, J.J.,Schiffer, C.A.,Fitzgerald, K.A.,Lin, K.,Royer, W.E.
Insights into interferon regulatory factor activation from the crystal structure of dimeric IRF5.
Nat.Struct.Mol.Biol., 15:1213-1220, 2008

PubMed Abstract: Interferon regulatory factors (IRFs) are essential in the innate immune response and other physiological processes. Activation of these proteins in the cytoplasm is triggered by phosphorylation of serine and threonine residues in a C-terminal autoinhibitory region, which stimulates dimerization, transport into the nucleus, assembly with the coactivator CBP/p300 and initiation of transcription. The crystal structure of the transactivation domain of pseudophosphorylated human IRF5 strikingly reveals a dimer in which the bulk of intersubunit interactions involve a highly extended C-terminal region. The corresponding region has previously been shown to block CBP/p300 binding to unphosphorylated IRF3. Mutation of key interface residues supports the observed dimer as the physiologically activated state of IRF5 and IRF3. Thus, phosphorylation is likely to activate IRF5 and other family members by triggering conformational rearrangements that switch the C-terminal segment from an autoinihibitory to a dimerization role.

PubMed: 18836453
DOI: 10.1038/nsmb.1496

実験手法

X-RAY DIFFRACTION (2 Å)