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Interactions of pleckstrin homology domains with membranes: adding back the bilayer via high throughput molecular dynamics

Abstract:

In this study we present a multi-scale molecular simulation pipeline for determining the favoured mode of interaction of a pleckstrin homology (PH) domain with a phosphatidyl-inositol-phosphate (PIP)-containing lipid bilayer. This allows us to predict PH/membrane interactions across a number of PH domains of known structure. Using the well-characterised GRP1 PH domain, we evaluate our methodology via comparison with available structural and biophysical data. Coarse-grained simulations are ana...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher version

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Publisher copy:
10.1016/j.str.2016.06.002

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
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Funding agency for:
Kalli, AC
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Funding agency for:
Sansom, MSP
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Grant:
Program for Leading Graduate Schools
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Grant:
Doctorate Student Grant-in-Aid Program
Publisher:
Elsevier (Cell Press) Publisher's website
Journal:
Structure Journal website
Publication date:
2016-01-01
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:d0454769-3d9a-40a7-919c-e5f2241c592a
Source identifiers:
625728
Local pid:
pubs:625728

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