[Interdomain interactions in aspartic proteases of higher organisms and their analogs in retroviral enzymes].
A continuous chain of hydrogen bonded groups, which forms cross-hands interaction between domains in molecules of pepsin-like enzymes, has been revealed. The chain contains a pair of 6 symmetrically related hydrogen bonds between main chain atoms and the two conserved water molecules. The peptide groups forming hydrogen bond with the inner oxygens of the active carboxyls are important elements of the chain. The so-called "fireman grip" hydrogen bonding, consisting of a pair of the two symmetrically related bonds, is an integral part of this system of interactions. One of the water molecules in this system has a zero accessibility and forms a very short hydrogen bond with the active site interacting peptide group. This chain connects tightly the two regions of domains which have a high correlation in conformational mobility. The retroviral enzymes have an abortive chain of the interdomain interaction in this region which is reduced to the "fireman grip" net.
Andreeva
N S
NS
Gurskaia
G V
GV
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D002245:Carbon Dioxide / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012190:Retroviridae / Q000201:enzymology*; D014867:Water / Q000737:chemistry
D010455:Peptides; D014867:Water; D002245:Carbon Dioxide; C041069:carboxyl radical; D016282:Aspartic Acid Endopeptidases