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Molecular dynamics simulations of the ligand-binding domain of an N-methyl-D-aspartate receptor.

Abstract:

The mechanism of partial agonism at N-methyl-D-aspartate receptors is an unresolved issue, especially with respect to the role of protein dynamics. We have performed multiple molecular dynamics simulations (7 x 20 ns) to examine the behavior of the ligand-binding core of the NR1 subunit with a series of ligands. Our results show that water plays an important role in stabilizing different conformations of the core and how a closed cleft conformation of the protein might be stabilized in the ab...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m512728200

Authors


Sansom, MS More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
The Journal of biological chemistry
Volume:
281
Issue:
18
Pages:
12736-12742
Publication date:
2006-05-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:c03c338c-44ab-4370-b208-951a2b09eb89
Source identifiers:
100190
Local pid:
pubs:100190

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