6F1E

Crystal structure of olive flounder [Paralichthys olivaceus] interferon gamma at 2.3 Angstrom resolution

6F1E の概要

• エントリーDOI: 10.2210/pdb6f1e/pdb
• 分子名称: Interferon gamma (2 entities in total)
• 機能のキーワード: interferon gamma, four-helix bundle, antiviral defense, immune system
• 由来する生物種: Paralichthys olivaceus (Bastard halibut)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40863.28

構造登録者

Kolenko, P.,Kolarova, L.,Zahradnik, J.,Schneider, B. (登録日: 2017-11-21, 公開日: 2018-05-23, 最終更新日: 2024-05-08)

主引用文献

Zahradnik, J.,Kolarova, L.,Parizkova, H.,Kolenko, P.,Schneider, B.
Interferons type II and their receptors R1 and R2 in fish species: Evolution, structure, and function.
Fish Shellfish Immunol., 79:140-152, 2018

PubMed Abstract: Interferon gamma (IFN-γ) is one of the key players in the immune system of vertebrates. The evolution and properties of IFN-γ and its receptors in fish species are of special interest as they point to the origin of innate immunity in vertebrates. We studied the phylogeny, biophysical and structural properties of IFN-γ and its receptors. Our phylogeny analysis suggests the existence of two groups of IFN-γ related proteins, one specific for Acanthomorpha, the other for Cypriniformes, Characiformes and Siluriformes. The analysis further shows an ancient duplication of the gene for IFN-γ receptor 1 (IFN- γR1) and the parallel existence of the duplicated genes in all current teleost fish species. In contrast, only one gene can be found for receptor 2, IFN- γR2. The specificity of the interaction between IFN- γ and both types of IFN- γR1 was determined by microscale thermophoresis measurements of the equilibrium dissociation constants for the proteins from three fish species. The measured preference of IFN- γ for one of the two forms of receptor 1agrees with the bioinformatic analysis of the coevolution between IFN- γ and receptor 1. To elucidate structural relationships between IFN-γ of fish and other vertebrate species, we determined the crystal structure of IFN-γ from olive flounder (Paralichthys olivaceus, PoliIFN-γ) at crystallographic resolution of 2.3 Å and the low-resolution structures of Takifugu rubripes, Oreochromis niloticus, and Larimichthys crocea IFN-γ by small angle X-ray diffraction. The overall PoliIFN-γ fold is the same as the fold of the other known IFN- γ structures but there are some significant structural differences, namely the additional C-terminal helix G and a different angle between helices C and D in PoliIFN-γ.

PubMed: 29742458
DOI: 10.1016/j.fsi.2018.05.008

実験手法

X-RAY DIFFRACTION (2.296 Å)