Govada, L;
Saridakis, E;
Kassen, SC;
Bin-Ramzi, A;
Morgan, RM;
Chain, B;
Helliwell, JR;
(2021)
X-ray crystallographic studies of RoAb13 bound to PIYDIN, a part of the N-terminal domain of C-C chemokine receptor 5.
IUCrJ
, 8
(Part 4)
pp. 678-683.
10.1107/S2052252521005340.
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Abstract
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.
| Type: | Article |
|---|---|
| Title: | X-ray crystallographic studies of RoAb13 bound to PIYDIN, a part of the N-terminal domain of C-C chemokine receptor 5 |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1107/S2052252521005340 |
| Publisher version: | http://dx.doi.org/10.1107/S2052252521005340 |
| Language: | English |
| Additional information: | This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
| Keywords: | Materials Science, CCR5 receptor, RoAb13, HIV entry, PIYDIN, antibodies, structure determination, viruses, X-ray crystallography, structural biology, CCR5, CRYSTALLIZATION, ANTIBODIES, REFINEMENT, OIL |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Infection and Immunity |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10131537 |
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