Anglia Ruskin Research Online (ARRO)
Browse
- No file added yet -

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

Download (786.48 kB)
journal contribution
posted on 2023-07-26, 15:27 authored by Lata Govada, Emmanuel Saridakis, Sean C. Kassen, Ahmad Bin-Ramzi, Rhodri M. Morgan, Benjamin Chain, John R. Helliwell, Naomi E. Chayen
C-C chemokine receptor 5 (CCR5) is a major co-receptor molecule used by HIV-1 to enter cells. This led to the hypothesis that stimulating an antibody response would block HIV with minimal toxicity. Here, X-ray crystallographic studies of the anti-CCR5 antibody RoAb13 together with two peptides were undertaken: one peptide is a 31-residue peptide containing the PIYDIN sequence and the other is the PIDYIN peptide alone, where PIYDIN is part of the N-terminal region of CCR5 previously shown to be important for HIV entry. In the presence of the longer peptide (the complete N-terminal domain), difference electron density was observed at a site within a hypervariable CDR3 binding region. In the presence of the shorter core peptide PIYDIN, difference electron density is again observed at this CDR3 site, confirming consistent binding for both peptides. This may be useful in the design of a new biomimetic to stimulate an antibody response to CCR5 in order to block HIV infection.

History

Refereed

  • Yes

Volume

8

Issue number

4

Page range

678-683

Publication title

IUCrJ

ISSN

2052-2525

Publisher

International Union of Crystallography

File version

  • Published version

Language

  • eng

Legacy posted date

2021-07-06

Legacy creation date

2021-07-06

Legacy Faculty/School/Department

Faculty of Science & Engineering

Usage metrics

    ARU Outputs

    Categories

    No categories selected

    Licence

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC