X-ray crystallographic studies of RoAb13 bound to PIYDIN, a part of the N-terminal domain of C-C chemokine receptor 5

C-C chemokine receptor 5 (CCR5) is a major co-receptor molecule used by HIV-1 to enter cells. This led the hypothesis that stimulating an antibody response would block HIV with minimal toxicity. Here, X-ray crystallographic studies of anti-CCR5 RoAb13 together two peptides were undertaken: one peptide 31-residue containing PIYDIN sequence and other PIDYIN alone, where part N-terminal region CCR5 previously shown be important for entry. In presence longer (the complete domain), difference electron density was observed at site within hypervariable CDR3 binding region. shorter core PIYDIN, again this site, confirming consistent both peptides. may useful in design new biomimetic stimulate order infection.