4LTB

Coiled-coil domain of TRIM25

4LTB の概要

• エントリーDOI: 10.2210/pdb4ltb/pdb
• 分子名称: Tripartite motif-containing 25 variant (2 entities in total)
• 機能のキーワード: coiled-coil, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43743.57

構造登録者

Pornillos, O.,Sanchez, J.G.,Okreglicka, K. (登録日: 2013-07-23, 公開日: 2014-02-05, 最終更新日: 2024-02-28)

主引用文献

Sanchez, J.G.,Okreglicka, K.,Chandrasekaran, V.,Welker, J.M.,Sundquist, W.I.,Pornillos, O.
The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.
Proc.Natl.Acad.Sci.USA, 111:2494-2499, 2014

PubMed Abstract: Tripartite motif (TRIM) proteins make up a large family of coiled-coil-containing RING E3 ligases that function in many cellular processes, particularly innate antiviral response pathways. Both dimerization and higher-order assembly are important elements of TRIM protein function, but the atomic details of TRIM tertiary and quaternary structure have not been fully understood. Here, we present crystallographic and biochemical analyses of the TRIM coiled-coil and show that TRIM proteins dimerize by forming interdigitating antiparallel helical hairpins that position the N-terminal catalytic RING domains at opposite ends of the dimer and the C-terminal substrate-binding domains at the center. The dimer core comprises an antiparallel coiled-coil with a distinctive, symmetric pattern of flanking heptad and central hendecad repeats that appear to be conserved across the entire TRIM family. Our studies reveal how the coiled-coil organizes TRIM25 to polyubiquitylate the RIG-I/viral RNA recognition complex and how dimers of the TRIM5α protein are arranged within hexagonal arrays that recognize the HIV-1 capsid lattice and restrict retroviral replication.

PubMed: 24550273
DOI: 10.1073/pnas.1318962111

実験手法

X-RAY DIFFRACTION (2.59 Å)