4b3n
Crystal structure of rhesus TRIM5alpha PRY/SPRY domainCrystal structure of rhesus TRIM5alpha PRY/SPRY domain
Structural highlights
Function[MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMedTripartite motif protein isoform 5 alpha (TRIM5alpha) is a potent antiviral protein that restricts infection by HIV-1 and other retroviruses. TRIM5alpha recognizes the lattice of the retrovirus capsid through its B30.2 (PRY/SPRY) domain in a species-specific manner. Upon binding, TRIM5alpha induces premature disassembly of the viral capsid and activates the downstream innate immune response. We have determined the crystal structure of the rhesus TRIM5alpha PRY/SPRY domain that reveals essential features for capsid binding. Combined cryo-electron microscopy and biochemical data show that the monomeric rhesus TRIM5alpha PRY/SPRY, but not the human TRIM5alpha PRY/SPRY, can bind to HIV-1 capsid protein assemblies without causing disruption of the capsid. This suggests that the PRY/SPRY domain alone constitutes an important pattern-sensing component of TRIM5alpha that is capable of interacting with viral capsids of different curvatures. Our results provide molecular insights into the mechanisms of TRIM5alpha-mediated retroviral restriction. Structural insight into HIV-1 capsid recognition by rhesus TRIM5alpha.,Yang H, Ji X, Zhao G, Ning J, Zhao Q, Aiken C, Gronenborn AM, Zhang P, Xiong Y Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18372-7. doi:, 10.1073/pnas.1210903109. Epub 2012 Oct 22. PMID:23091002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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