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X-ray crystallography studies of RoAb13 bound to PIYDIN, a part of the CCR5 N terminal domain

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Title: X-ray crystallography studies of RoAb13 bound to PIYDIN, a part of the CCR5 N terminal domain
Authors: Govada, L
Saridakis, E
Kassen, SC
Bin-Ramzi, A
Morgan, RM
Chain, B
Helliwell, JR
Chayen, N
Item Type: Journal Article
Abstract: C-C chemokine receptor 5 (CCR5) is a major co-receptor molecule used by HIV-1 to enter cells. This opens the hypothesis that stimulating an antibody response would block HIV with minimal toxicity. We have undertaken X-ray crystallography studies of the anti-CCR5 antibody RoAb13 together with two peptides, one a 31 peptide containing PIYDIN and the other a PIDYIN 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), we observed difference electron density 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 designing a new biomimetic to stimulate an antibody response to CCR5 in order to block HIV infection.
Date of Acceptance: 14-May-2021
URI: http://hdl.handle.net/10044/1/89922
ISSN: 2052-2525
Publisher: International Union of Crystallography
Journal / Book Title: IUCrJ
Copyright Statement: This paper is embargoed until publication. Once published it will be available fully open access.
Sponsor/Funder: Engineering & Physical Science Research Council (EPSRC)
Funder's Grant Number: EP/G027005/1
Keywords: 0202 Atomic, Molecular, Nuclear, Particle and Plasma Physics
0204 Condensed Matter Physics
0306 Physical Chemistry (incl. Structural)
Publication Status: Accepted
Embargo Date: publication subject to indefinite embargo
Appears in Collections:Department of Metabolism, Digestion and Reproduction
Faculty of Natural Sciences