Discovering the interaction propensities of amino acids and nucleotides from protein-RNA complexes.
With the availability of many genome sequences, the mining of biological data is attracting much attention, most of it limited to the sequences of macromolecules. Sequence data are easy to analyze as they can be treated as strings of characters, whereas the structure of a macromolecule is much more complex. We developed a set of algorithms to analyze the structures of protein-RNA complexes at the atomic level and used them to analyze protein-RNA interactions using structural data on 51 protein-RNA complexes. The analysis revealed, among other things, that: (1) polar and charged amino acids have a strong tendency to interact with nucleotides, (2) arginine and asparagine tend to hydrogen bond with uracil, and (3) histidine favors uracil in water-mediated bonding with RNA. We analyzed a large set of structural data of protein-RNA complexes involving water-mediated hydrogen bonds as well as direct hydrogen bonds. The interaction patterns discovered from the analysis provide useful information for predicting the structure of RNA that binds proteins, and of proteins that bind RNA.
Jeong
Euna
E
School of Computer Science and Engineering, Inha University, Incheon 402-751, Korea.
Kim
Hyunwoo
H
Lee
Seong-Wook
SW
Han
Kyungsook
K
D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry*; D001216:Asparagine / Q000737:chemistry; D020029:Base Pairing; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009711:Nucleotides / Q000737:chemistry; D011487:Protein Conformation; D012313:RNA / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry*; D014498:Uracil / Q000737:chemistry
D000596:Amino Acids; D009711:Nucleotides; D016601:RNA-Binding Proteins; D014498:Uracil; D012313:RNA; D001216:Asparagine