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In silico mutation of cysteine residues in the ligand-binding domain of an N-methyl-D-aspartate receptor.

Abstract:

The precise nature of redox modulation of N-methyl-d-aspartate (NMDA) receptors is still unclear, although it is thought to be related to the formation and breaking of disulfide bonds. Recent structural data demonstrated the way in which disulfide bonds in the ligand-binding core of the NR1 subunit are arranged. However, the structures were not able to reconcile existing experimental data that examined the effects of mutating these cysteine residues. We have used molecular dynamics (MD) simul...

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Publication status:
Published

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Publisher copy:
10.1021/bi061462d

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Biochemistry
Volume:
46
Issue:
8
Pages:
2136-2145
Publication date:
2007-02-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:6088671b-7b42-4036-9ef6-e6e567e9439b
Source identifiers:
99979
Local pid:
pubs:99979

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