Journal article icon

Journal article

Molecular dynamics studies of AChBP with nicotine and carbamylcholine: the role of water in the binding pocket.

Abstract:

The acetylcholine-binding protein (AChBP) is homologous to the ligand-binding domain of the nicotinic acetylcholine receptor (nAChR) and other members of the Cys-loop family of neurotransmitter receptors. The high-resolution X-ray structures of AChBP mean it has been used as a model from which to understand agonist and antagonist binding to nAChRs. We present here a molecular dynamics (MD) study of AChBP with nicotine and carbamylcholine bound. Our results suggest that the ligand imposes rigi...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1093/protein/gzm029

Authors


Sansom, MS More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Protein engineering, design and selection : PEDS
Volume:
20
Issue:
7
Pages:
353-359
Publication date:
2007-07-05
DOI:
EISSN:
1741-0134
ISSN:
1741-0126
URN:
uuid:f646a1ac-23c5-40ab-82e0-f778ee2d5523
Source identifiers:
100150
Local pid:
pubs:100150

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP