Biopolym. Cell. 2000; 16(6):515-524.
Structure and Function of Biopolymers
Structure modeling of the COOH-terminal cytokine-like module of the mammalian cytoplasmic tyrosyl-tRNA synthetase
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680 - Institute of Cell Biology and Genetic Engineering, NAS of Ukraine
148, Akademika Zabolotnogo Str., Kyiv, Ukraine, 03680
Abstract
COOH-terminal module (C-module) of cytoplasmic tyrosyl-tRNA synthetases from chordate and insects is homologous to the mammalian cytokine EMAP II (52.7 % identity) and in free form has similar biological properties in experiments in vitro. The main part of C-module is a domain with «OB-fold» type of structure (B-domain, residues Val363-Lys470), containing five β-strands, which are characteristic for this fold type. Like some other «OB-fold»-containing domains C-module has affinity to nucleic acids. By using comparative homology modeling methods the C-module structure model of bovine (Bos taurus) tyrosyl-tRNA synthetase is created. The comparison of C-module model with anticodon-binding domains of aspartyl- and lysyl-tRNA synthetases allows to predict the interacting surface with RNA and some functionally important amino acid residues. The C-module structure model will help to study further the tyrosyl-tRNA synthetase structure and functions, its interaction with tRNATyr, and cytokine-like properties of the free C-module.
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