期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 47, 期 -, 页码 23-29出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2017.04.005
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资金
- US National Institutes of Health grant [AI070042]
- Francis Crick Institute
- Cancer Research UK [FC001061]
- UK Medical Research Council [FC001061]
- Wellcome Trust [FC001061]
- The Francis Crick Institute [10061] Funding Source: researchfish
Retroviral DNA integration takes place in the context of the intasome nucleoprotein complex. X-ray crystal structures of functional spumaviral intasomes were previously revealed to harbor a homotetramer of integrase, and it was generally believed that integrase tetramers catalyzed the integration of other retroviruses. The elucidation of new structures from four different retroviruses over the past year has however revealed this is not the case. The number of integrase molecules required to construct the conserved intasome core structure differs between viral species. While four subunits suffice for spumaviruses, alpha- and beta-retroviruses require eight and the lentiviruses use up to sixteen. Herein we described these alternative architectures, highlighting both evolutionary and structural constraints that result in the different integrase-DNA stoichiometries across Retroviridae.
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