This study provides the molecular bases for recognition, binding and specificity of peptide transporters for dipeptides with a charged amino acid residue at the N-terminal position.
The X-ray crystal structure of the peptide transporter YePEPT from the bacterium Yersinia enterocolitica together with functional studies have unveiled the molecular bases for recognition, binding and specificity of dipeptides with a charged amino acid residue at the N-terminal position.
We aim to establish the evidence base for the recognition and management of obstetric anal sphincter injury (OASI) and to compare this with current practice amongst UK obstetricians and coloproctologists.
Here, structural bases for oseltamivir recognition by group-1 NA8, Nandand group-2 Nareare highlighted by the ScrewFit algorithm for quantitative structure comparison.
Intensive research in this laboratory over the last 19 years has aimed at understanding the molecular bases for immune recognition of botulinum neurotoxin, types A and B and the role of anti-toxin immune responses in defense against the toxin.
The molecular bases for the recognition of biotrophs by plants outside the purview of gene-for-gene systems are still elusive.
In summary, the crystal structure of YePEPT together with structure-function studies have provided the molecular bases for the recognition, binding and specificity of charged amino acid residues at the N-terminal position of dipeptides by peptide transporters of the POT family.
For example, the first base pair in the archaeal M. jannashii (Mj) tyrosine tRNA is C1 G72, which in addition to the discriminator base A73 is required for recognition of the cognate tRNA by the Mj tyrosyl-tRNA synthetase.
These residues may all represent weak code, if they are used for base recognition.
Evaluation of the available crystallographic structures point to the presence of a conserved water molecule which could have importance for base recognition within class II enzymes, a property that can be explored in future drug design efforts.
