TRIM5 polyclonal antibody

TRIM5a is a 493 amino acid member of the large tripartite motif protein (TRIM) family. TRIM proteins are composed of three zinc-binding domains, a RING, a B-box 2 and a coiled-coil domain, and they use homomultimerization to identify different cell compartments. Some TRIM proteins, such as TRIM5a, also possess a carboxy-terminal B30.2 (SPRY) domain and localize to the cytoplasm. TRIM5a mediates innate intracellular retroviral resistance, which is dependent on its carboxy-terminal domain. The three variable regions of the B30.2 domain form loops on one side of the B30.2 core structure of TRIM5a which may form a binding surface for the virus. TRIM5a trimerization plays a major role in its affinity for the retroviral capsid, and in its ability to inhibit virus infection. The linker region between the coiled-coil and B30.2 domains of TRIM5a is required for this trimerization. TRIM5a blocks infection after the virus has entered the cell.