title: Interface of apoptotic protein complexes has distinct properties.
abstract: Apoptosis is a programmed mechanism of cell death that is a normal component of development and health of multi-cellular organisms. In this study, we ask if interface properties of apoptotic protein complexes are different from protein complexes in general. We find that although in apoptotic protein complexes the overall distribution of interface size, surface complementarity, hydrogen bonding, hydrophobicity are similar to general interface properties, apoptotic complexes tend to have more fragmented interfaces and different secondary structural preferences. The statistics on the number of interfaces where specific amino acid(s) occur with significantly enhanced frequency suggest that Arg, Met and Asp are most important functional residues. The role of Met is believed to be unique, as evidenced from the existing data on hot spot potential of residues. These findings together provide insight into the possible role of various physico-chemical attributes at the protein interface in regulation of the apoptosis process.
authors.affiliation: Supercomputer Education and Research Centre, Bangalore, India Bioinformatics Centre, Indian Institute of Science, Bangalore, India.
authors.forename: Pralay
authors.initials: P
authors.lastname: Mitra
authors.forename: Riddhiman
authors.initials: R
authors.lastname: Dhar
authors.forename: Debnath
authors.initials: D
authors.lastname: Pal
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D017209:Apoptosis; D051017:Apoptosis Regulatory Proteins / Q000378:metabolism*; D030562:Databases, Protein; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D046912:Multiprotein Complexes / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012492:Salts
chemical_list: D000596:Amino Acids; D051017:Apoptosis Regulatory Proteins; D046912:Multiprotein Complexes; D012492:Salts