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The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer

Sanchez, Jacint G. ; Okreglicka, Katarzyna ; Chandrasekaran, Viswanathan ; Welker, Jordan M. ; Sundquist, Wesley I. ; Pornillos, Owen

Proceedings of the National Academy of Sciences - PNAS, 2014-02, Vol.111 (7), p.2494-2499 [Periódico revisado por pares]

United States: National Academy of Sciences

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Título:
The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer
Autor: Sanchez, Jacint G. ; Okreglicka, Katarzyna ; Chandrasekaran, Viswanathan ; Welker, Jordan M. ; Sundquist, Wesley I. ; Pornillos, Owen
Assuntos: Antivirals ; Base Sequence ; Biochemistry ; Biological Sciences ; Capsid ; Cellular biology ; Crosslinking ; Crystal structure ; Crystallography ; Crystallography, X-Ray ; Dimerization ; Dimers ; Disulfides ; Evolution, Molecular ; Fluorometry ; HIV ; Human immunodeficiency virus ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary - genetics ; Proteins ; Ribonucleic acid ; RNA ; Rosaniline Dyes ; Sequence Analysis, DNA ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Tripartite Motif Proteins ; Ubiquitin-Protein Ligases - chemistry ; Ubiquitin-Protein Ligases - genetics ; Ubiquitins ; Ultracentrifugation
É parte de: Proceedings of the National Academy of Sciences - PNAS, 2014-02, Vol.111 (7), p.2494-2499
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Author contributions: W.I.S. and O.P. designed research; J.G.S., K.O., V.C., J.M.W., and O.P. performed research; J.G.S., K.O., V.C., J.M.W., W.I.S., and O.P. analyzed data; and J.G.S., K.O., V.C., W.I.S., and O.P. wrote the paper.
1J.G.S. and K.O. contributed equally to this work.
Edited by Alfonso Mondragon, Northwestern University, Evanston, IL, and accepted by the Editorial Board January 8, 2014 (received for review October 8, 2013)
Descrição: 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.
Editor: United States: National Academy of Sciences
Idioma: Inglês

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The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer

Sanchez, Jacint G. ; Okreglicka, Katarzyna ; Chandrasekaran, Viswanathan ; Welker, Jordan M. ; Sundquist, Wesley I. ; Pornillos, Owen

United States: National Academy of Sciences

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