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Functional interplay between the B-box 2 and the B30.2(SPRY) domains of TRIM5α
- Source :
- Virology. (2):234-244
- Publisher :
- Elsevier Inc.
-
Abstract
- The retroviral restriction factors, TRIM5alpha and TRIMCyp, consist of RING and B-box 2 domains separated by a coiled coil from carboxy-terminal domains. These carboxy-terminal domains (the B30.2(SPRY) domain in TRIM5alpha and the cyclophilin A domain in TRIMCyp) recognize the retroviral capsid. Here we show that some B-box 2 changes in TRIM5alpha, but not in TRIMCyp, resulted in decreased human immunodeficiency virus (HIV-1) capsid binding. The phenotypic effects of these B-box 2 changes on the restriction of retroviral infection depended on the potency of restriction and the affinity of the TRIM5alpha interaction with the viral capsid, two properties specified by the B30.2(SPRY) domain. Thus, some alterations in the TRIM5alpha B-box 2 domain apparently affect the orientation or conformation of the B30.2(SPRY) domain, influencing capsid recognition.
- Subjects :
- Ubiquitin-Protein Ligases
viruses
Plasma protein binding
Biology
medicine.disease_cause
Article
Antiviral Restriction Factors
Tripartite Motif Proteins
Cyclophilin A
Retrovirus
Protein structure
Virology
medicine
Animals
Humans
Cyclophilin
Trimer
B30.2(SPRY)
Coiled coil
Genetics
N-MLV
Restriction factor
Proteins
Simian immunodeficiency virus
biology.organism_classification
Protein Structure, Tertiary
Capsid
HIV-1
Capsid Proteins
Simian Immunodeficiency Virus
B-box 2
Moloney murine leukemia virus
Carrier Proteins
TRIMCyp
HeLa Cells
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 00426822
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Virology
- Accession number :
- edsair.doi.dedup.....7d136cb5ed796d7d57584e678092e29e
- Full Text :
- https://doi.org/10.1016/j.virol.2007.04.022