期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 7, 页码 2494-2499出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1318962111
关键词
antiparallel dimer; disulfide crosslinking; X-ray crystallography
资金
- University of Virginia School of Medicine
- National Institutes of Health [P50 GM082545, T32 GM008136]
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 polyubi-quitylate the RIG-I/viral RNA recognition complex and how dimers of the TRIM5 alpha protein are arranged within hexagonal arrays that recognize the HIV-1 capsid lattice and restrict retroviral replication.
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