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

被引:158
作者
Sanchez, Jacint G. [1 ,2 ]
Okreglicka, Katarzyna [1 ,2 ]
Chandrasekaran, Viswanathan [3 ]
Welker, Jordan M. [1 ,2 ]
Sundquist, Wesley I. [3 ]
Pornillos, Owen [1 ,2 ]
机构
[1] Univ Virginia, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA
[2] Univ Virginia, Myles H Thaler Ctr AIDS & Human Retrovirus Res, Charlottesville, VA 22908 USA
[3] Univ Utah, Dept Biochem, Salt Lake City, UT 84112 USA
基金
美国国家卫生研究院;
关键词
antiparallel dimer; disulfide crosslinking; X-ray crystallography; TRIM5-ALPHA PRYSPRY DOMAIN; HIV-1 CAPSID RECOGNITION; RETROVIRAL RESTRICTION; RIG-I; MONKEY TRIM5-ALPHA; RHESUS TRIM5-ALPHA; BINDING; RING; PROTEINS; ASSOCIATION;
D O I
10.1073/pnas.1318962111
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:2494 / 2499
页数:6
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