4b3n | pdb_00004b3n

Crystal structure of rhesus TRIM5alpha PRY/SPRY domain

spinqualitylabelsall models 4b3n, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b3n is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLC, MES Related: 1anf, 1dmb, 1ez9, 1ezo, 1ezp, 1fqa, 1fqb, 1fqc, 1fqd, 1iud, 1jvx, 1jvy, 1jw4, 1jw5, 1lax, 1lls, 1mdp, 1mdq, 1mpb, 1mpc, 1mpd, 1n3w, 1n3x, 1nl5, 1nmu, 1omp, 1peb, 1r6z, 1svx, 1t0k, 1y4c, 1ytv, 1ziu, 1zjl, 1zkb, 1zmg, 2d21, 2h25, 2vgq, 2xz3, 3mbp, 4auf, 4aug, 4auh, 4mbp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 PubMed Tripartite 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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