CH/pi interactions as demonstrated in the crystal structure of guanine-nucleotide binding proteins, Src homology-2 domains and human growth hormone in complex with their specific ligands.
The CH/pi interaction is a weak attractive molecular force occurring between CH groups and pi-systems. Possibility has been examined for the role of CH/pi interaction, by use of a computer program, in the crystallographic data of several guanine-nucleotide binding proteins, src homology-2 domains and human growth hormone complexed with their specific ligands. Short CH/pi contacts have been found in every case where cohesive forces are expected. Comparison of the structures of functionary related proteins has shown that mutation may occur but necessary CH/pi interactions are conserved. A considerable part of the non-polar interactions, broadly ascribed in the past to the van der Waals interaction or the so-called hydrophobic effect, has been suggested to be attributed to a more specific attractive force, the CH/pi interaction.
Umezawa
Y
Y
Institute of Microbial Chemistry, Tokyo, Japan.
Nishio
M
M
D000818:Animals; D006224:Cricetinae; D018360:Crystallography, X-Ray; D019204:GTP-Binding Proteins / Q000737:chemistry*; D019382:Human Growth Hormone / Q000737:chemistry*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D010444:Peptide Elongation Factor Tu / Q000737:chemistry; D016283:Proto-Oncogene Proteins p21(ras) / Q000737:chemistry; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D015293:Transducin / Q000737:chemistry; D018909:src Homology Domains
D008024:Ligands; D019382:Human Growth Hormone; D012259:Ribonuclease, Pancreatic; D019204:GTP-Binding Proteins; D010444:Peptide Elongation Factor Tu; D015293:Transducin; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)