Role of electrostatic interactions for ligand recognition and specificity of peptide transporters.

ABSTRACT:

Background

Peptide transporters are membrane proteins that mediate the cellular uptake of di- and tripeptides, and of peptidomimetic drugs such as β-lactam antibiotics, antiviral drugs and antineoplastic agents. In spite of their high physiological and pharmaceutical importance, the molecular recognition by these transporters of the amino acid side chains of short peptides and thus the mechanisms for substrate binding and specificity are far from being understood.

Results

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. In wild-type YePEPT

SUBMITTER: Boggavarapu R 

PROVIDER: S-EPMC4527243 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature