TRIM5alpha

18Citations
Citations of this article
21Readers
Mendeley users who have this article in their library.
Get full text

Abstract

TRIM5α protein blocks retroviral replication at early postentry stage reducing the accumulation of reverse transcriptase products. TRIM5α proteins of Old World primates restrict HIV-1 infection whereas TRIM5α proteins of most New World monkeys restrict SIVmac infection. TRIM5α protein has a RING domain, B-box 2 domain, coiled-coil domain, and PRYSPRY domain. The PRYSPRY domain of TRIM5α determines viral specificity and restriction potency by mediating recognition of the retroviral capsid. The coiled-coil domain is essential for TRIM5α oligomerization, which contributes to binding avidity for the viral capsid. The RING domain and B-box 2 domain are required for efficient restriction activity of TRIM5α protein but the mechanisms remain to be defined. © 2009 Springer-Verlag Berlin Heidelberg.

Cite

CITATION STYLE

APA

Song, B. (2009). TRIM5alpha. Current Topics in Microbiology and Immunology. Springer Verlag. https://doi.org/10.1007/978-3-642-02175-6_3

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free