[Principal role of large polar residue clusters of RNA-binding proteins in the formation of complexes with RNA].
Three-dimensional crystallographic data for a number of protein-RNA complexes were used to study the localization of protein binding regions at the protein surface. The set consists of ten non-homologous complexes, which include 20 independent binding sites. In most sites the contact interaction of polar residue side groups makes a significant contribution to protein binding regions. It was discovered that binding polar residues are localized essentially inside one largest cluster of polar residues at the protein surface. In fact, for fifteen regions 80.5% of polar binding residues were situated in such a large cluster. This result supports strongly a definitive role of the largest polar cluster in the recognition of the major groove of B-DNA by the protein transcription and regulatory factors, which has been recently disclosed by us. Therefore, at present one can suggest that the largest cluster of protein polar residues could play a key role in the formation of binding sites of proteins with DNA and RNA.
Chirgadze
Iu N
IuN
Larionova
E A
EA
D000818:Animals; D001665:Binding Sites; D004247:DNA / Q000737:chemistry; D011485:Protein Binding; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism
D016601:RNA-Binding Proteins; D012313:RNA; D004247:DNA