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TitleCrystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain.
Journal, issue, pagesBMC Struct Biol, Vol. 8, Page 11, Year 2008
Publish dateFeb 28, 2008
AuthorsJane A Potter / Richard E Randall / Garry L Taylor /
PubMed AbstractBACKGROUND: IPS-1/MAVS/VISA/Cardif is an adaptor protein that plays a crucial role in the induction of interferons in response to viral infection. In the initial stage of the intracellular antiviral ...BACKGROUND: IPS-1/MAVS/VISA/Cardif is an adaptor protein that plays a crucial role in the induction of interferons in response to viral infection. In the initial stage of the intracellular antiviral response two RNA helicases, retinoic acid inducible gene-I (RIG-I) and melanoma differentiation-association gene 5 (MDA5), are independently able to bind viral RNA in the cytoplasm. The 62 kDa protein IPS-1/MAVS/VISA/Cardif contains an N-terminal caspase activation and recruitment (CARD) domain that associates with the CARD regions of RIG-I and MDA5, ultimately leading to the induction of type I interferons. As a first step towards understanding the molecular basis of this important adaptor protein we have undertaken structural studies of the IPS-1 MAVS/VISA/Cardif CARD region.
RESULTS: The crystal structure of human IPS-1/MAVS/VISA/Cardif CARD has been determined to 2.1A resolution. The protein was expressed and crystallized as a maltose-binding protein (MBP) fusion protein. The MBP and IPS-1 components each form a distinct domain within the structure. IPS-1/MAVS/VISA/Cardif CARD adopts a characteristic six-helix bundle with a Greek-key topology and, in common with a number of other known CARD structures, contains two major polar surfaces on opposite sides of the molecule. One face has a surface-exposed, disordered tryptophan residue that may explain the poor solubility of untagged expression constructs.
CONCLUSION: The IPS-1/MAVS/VISA/Cardif CARD domain adopts the classic CARD fold with an asymmetric surface charge distribution that is typical of CARD domains involved in homotypic protein-protein interactions. The location of the two polar areas on IPS-1/MAVS/VISA/Cardif CARD suggest possible types of associations that this domain makes with the two CARD domains of MDA5 or RIG-I. The N-terminal CARD domains of RIG-I and MDA5 share greatest sequence similarity with IPS-1/MAVS/VISA/Cardif CARD and this has allowed modelling of their structures. These models show a very different charge profile for the equivalent surfaces compared to IPS-1/MAVS/VISA/Cardif CARD.
External linksBMC Struct Biol / PubMed:18307765 / PubMed Central
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-2vgq:
Crystal Structure of Human IPS-1 CARD
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM/TRANSPORT / IPS1/MAVS/VISA/CARDIF / CASPASE ACTIVATION / CASPASE RECRUITMENT DOMAIN / INNATE IMMUNITY / FUSION PROTEIN / SUGAR TRANSPORT / TRANSPORT / IMMUNE SYSTEM / CHIMERA / IMMUNE SYSTEM-TRANSPORT complex

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