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Atomistic mechanism of transmembrane helix association

Abstract:

Transmembrane helix association is a fundamental step in the folding of helical membrane proteins. The prototypical example of this association is formation of the glycophorin dimer. While its structure and stability have been well-characterized experimentally, the detailed assembly mechanism is harder to obtain. Here, we use all-atom simulations within phospholipid membrane to study glycophorin association. We find that initial association results in the formation of a non-native intermediat...

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Publication status:
Published
Peer review status:
Peer reviewed

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Authors


Domański, J More by this author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Stansfeld, PJ More by this author
Publisher:
Public Library of Science Publisher's website
Journal:
PLoS Computational Biology Journal website
Volume:
16
Issue:
6
Article number:
e1007919
Publication date:
2020-06-04
Acceptance date:
2020-04-30
DOI:
EISSN:
1553-7358
ISSN:
1553-734X
Pubs id:
1102448
Local pid:
pubs:1102448
Language:
English
Keywords:

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