Structure of the BBox-Coiled-coil region of Rhesus Trim5alpha

Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice.

TRIM5/cyclophilin A fusion protein/T4 Lysozyme chimera

MAHHHHHHSAALEVLFQGPGPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCKDSQEHRGHHTFLMEEVAQEYHVKLQTA
LEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQT
QYMRELISELEHRLQGSMMDLLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRDAAAEESPVLLAMNIF
EMLRIDEGLRLKIYKNTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKL
KPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

10% PEG4000, 20% Glycerol, 0.2M monosaccharides, 0.1M Bis/Tris pH 8.5

Medical Research Council (MRC, United Kingdom)

Dimer confirmed by size exclusion chromatography

Trim protein Coiled-coil scaffold retroviral restriction factor, ANTIVIRAL PROTEIN

PEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIRE
EKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISELEHRLQGSMMD
LLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRDAAAEESPVLLA

MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDA
YKNL